Total whey protein is composed of a mixture of proteins with different structures and functions. Separation into fractions is based on the different mobility of proteins in the separating medium under the action of an electric field.The following fractions are isolated by electrophoresis:
albumin and alpha1, alpha2, beta and gamma globulins.
GLOBULINS
Unlike albumin, globulins are not water-soluble, but soluble in weak saline solutions.
a1-GLOBULINS
This fraction includes a variety of proteins. a1-globulins are highly hydrophilic and low in molecular weight. Therefore, with kidney pathology, they are easily lost in the urine. However, their loss does not significantly affect oncotic blood pressure, because their content in blood plasma is low.
Functions of a1-globulins:
- Transport. They transport lipids, while forming complexes with them - lipoproteins. Among the proteins of this fraction there is a special protein intended for the transport of the thyroid hormone thyroxine - thyroxine-binding protein.
- Participation in the functioning of the blood coagulation system and the complement system - this fraction also contains some blood coagulation factors and components of the complement system.
- Regulatory function. Some proteins of the α1-globulin fraction are endogenous inhibitors of proteolytic enzymes. The highest plasma concentration of a1-antitrypsin. Its content in plasma is from 2 to 4 g / l (very high), molecular weight - 58-59 kDa. Its main function is to inhibit elastase, an enzyme that hydrolyzes elastin (one of the main proteins of connective tissue). a1-antitrypsin is also an inhibitor of proteases: thrombin, plasmin, trypsin, chymotrypsin and some enzymes of the blood coagulation system. The amount of this protein increases in inflammatory diseases, during the processes of cellular decay, decreases in severe liver diseases. This decrease is the result of a violation of the synthesis of a1-antitrypsin, and it is associated with excessive cleavage of elastin. There is a congenital deficiency of a1-antitrypsin. It is believed that the lack of this protein contributes to the transition of acute diseases to chronic ones.
a2-GLOBULINS.
High molecular weight proteins. This fraction contains regulatory proteins, blood coagulation factors, components of the complement system, transport proteins. This includes ceruloplasmin. This protein has 8 copper binding sites. It is a carrier of copper, and also ensures the constancy of copper content in various tissues, especially in the liver. Haptoglobins. The content of these proteins is approximately 1/4 of all a2-globulins. Haptoglobin forms specific complexes with hemoglobin released from erythrocytes during intravascular hemolysis. Due to the high molecular weight of these complexes, they cannot be excreted by the kidneys. This prevents the body from losing iron.
Complexes of hemoglobin with haptoglobin are destroyed by cells of the reticuloendothelial system (cells of the mononuclear phagocyte system), after which globin is split into amino acids, heme is destroyed to bilirubin and excreted by bile, and iron remains in the body and can be reused. The a2-macroglobulin also belongs to the same fraction. The molecular weight of this protein is 720 kDa, the concentration in blood plasma is 1.5-3 g / l. It is an endogenous inhibitor of proteinases of all classes, and also binds the hormone insulin. The half-life of a2-macroglobulin is very short - 5 minutes. This is a universal "cleaner" of blood, complexes "a2-macroglobulin-enzyme" are able to absorb immune peptides, for example, interleukins, growth factors, tumor necrosis factor, and remove them from the bloodstream.
C1-inhibitor - a glycoprotein, is the main regulatory link in the classical pathway of complement activation (CPA), is able to inhibit plasmin, kallikrein. With a lack of C1-inhibitor, angioedema develops.
b-GLOBULINS
This fraction includes some proteins of the blood coagulation system and the vast majority of components of the complement activation system (from C2 to C7).
The basis of the β-globulin fraction is low density lipoproteins (LDL), transferin (an iron carrier protein), hemopexin (binds heme, which prevents its excretion by the kidneys and loss), complement components (involved in immune reactions), and some immunoglobulins.
g-GLOBULINS
This faction contains mainly ANTIBODIES. The function of antibodies is to protect the body from foreign agents (bacteria, viruses, foreign proteins), which are called ANTIGENS.
Immunoglobulins, (in descending order - IgG, IgA, IgM, IgE), functionally representing antibodies that provide the body's humoral immune defense against infections and foreign substances.
Only IgG and IgM are able to activate the complement system. C-reactive protein is also able to bind and activate the C1 component of complement, but this activation is counterproductive and leads to the accumulation of anaphylotoxins. The accumulated anaphylotoxins cause allergic reactions.
Cryoglobulins also belong to the group of gamma globulins. These are proteins that can precipitate when whey is cooled. Healthy people do not have them in serum. They appear in patients with rheumatoid arthritis and multiple myeloma.
Level increase: Albumin:. Dehydration; Shock;
Alpha1-globulin fraction: Pregnancy (3rd trimester); Pathology of the liver parenchyma; Acute and chronic inflammatory processes (infections and rheumatic diseases); Tumors; Trauma and surgery; Taking androgens.
Alpha 2-Globulin Fraction: Pregnancy; Nephrotic syndrome, Hepatitis, Liver cirrhosis, Taking estrogens and oral contraceptives, Malignant tumors, Tissue necrosis, Chronic inflammatory process.
Beta-globulin fraction: Pregnancy; Primary and secondary hyperlipoproteinemia; Monoclonal gammopathies; Taking estrogens, iron deficiency anemia (increased transferrin); Obstructive jaundice.
Decreased levels: Albumin: Eating disorders; Malabsorption syndrome; Diseases of the liver and kidneys; Tumors; Collagenoses; Burns; Overhydration; Bleeding; Analbuminemia; Pregnancy.
Alpha1-globulin fraction: Hereditary alpha1-antitrypsin deficiency; Tangier disease.
Alpha2-globulin fraction: pancreatitis, burns, trauma; Decreased haptoglobin (hemolysis of various etiologies, pancreatitis, sarcoidosis); Beta-globulin fraction: Hypo-b-lipoproteinemia; IgA deficiency; Fraction of gamma globulin: Immunodeficiency states; Taking glucocorticoids; Pregnancy.
Norm: adults
Albumin 56-66%
alpha-1-globulins 3.5-6%
alpha-2-globulins 6-10%
beta globulins 8-18%
gamma globulins 15-25%
Protein and protein fractions of blood serum - the first, with which the list of results of a biochemical blood test begins. The component that the patient who receives the test sheet for his hands first of all pays attention to.
The phrase "total protein" usually does not raise any questions - many perceive the concept of "protein" simply: it is familiar, often found in life and everyday life. It is different with the so-called "protein fractions" - albumin, globulins, fibrinogen. These names are unusual and somehow not associated with protein at all. In this article, we will tell you what protein fractions are, what functions they perform in the body, how, based on their values, it is possible to identify dangerous pathologies in the state of human health.
Albumin
Albumin is quite common in the body and accounts for 55-60% of all protein compounds. It is mainly found in two fluids - in blood serum and cerebrospinal fluid. Accordingly, "serum albumin" - a blood plasma protein - and spinal albumin are secreted. This division is arbitrary, it is used for the convenience of physicians and does not have much significance for medical science, since the origin of spinal albumin is closely related to serum albumin.
Albumin is formed in the liver - it is an endogenous product of the body.
The main function of albumin is to regulate blood pressure.
Due to the migration of water molecules, which is provided by albumin, colloid-osmotic determination of blood pressure occurs. The figure below the paragraph clearly shows exactly how this happens. A decrease in the size of red blood cells reduces blood volume in general and makes the heart work more often to compensate for the lost dimensions of normal blood volume. An increase in red blood cells leads to the opposite situation - the heart works less often, the blood pressure drops.
The secondary function of albumin is no less important - the transport of various substances in the human body. This is the movement of all substances that do not dissolve in water, including such dangerous toxins as heavy metal salts, bilirubin and its fractions, hydrochloric and sulfuric acid salts. Albumin also promotes the elimination of antibiotics and their breakdown products from the body.
The main physical difference between albumin and globulins and fibrinogen is its ability to dissolve in water. A minor physical difference is its molecular weight, which is much lower than that of other whey proteins.
Globulins
Globulins, unlike albumin, dissolve poorly in water, better in slightly salted and slightly alkaline solutions. Globulins, like albumins, are synthesized in the liver, but not only - most of them appear due to the work of the organs of the immune system.
These proteins are actively involved in the so-called immune response - a response to an external or internal threat to the health of the human body.
Globulins are divided into protein fractions: "alpha", "beta" and "gamma".
Modern biochemistry divides alpha globulins into two subspecies - alpha-1 and alpha-2. With external similarity, proteins differ quite strongly among themselves. This primarily concerns their functions.
- Alpha 1 - inhibits proteolytic active substances, catalysts of biochemical reactions; oxidizes the area of inflammation of body tissues; promotes the transport of thyroxine (thyroid hormone) and cortisol (adrenal hormone).
- Alpha 2 - is responsible for the regulation of immunological reactions, the formation of a primary response to an antigen; helps to bind bilirubin; promotes the transfer of "bad" cholesterol; increases the antioxidant capacity of body tissues.
Beta globulins, like alpha, have two subspecies - beta-1 and beta-2. The differences between these protein fractions of blood are not so significant as to be considered separately. Beta globulins are more closely involved than the alpha globulins in the immune system. The main task of the "beta" group globulins is to promote lipid metabolism.
Gamma globulin is the main protein of the immune system; without it, the work of humoral immunity is impossible. This protein is part of all antibodies produced by our body to fight against enemy antigenic agents.
Fibrinogen
The main feature of fibrinogen is its participation in blood clotting processes.
Therefore, the values of the analyzes associated with this type of protein are important to everyone who is going to go to surgery, expecting a baby or ready to become pregnant.
The norms of the content of protein fractions in the blood and pathology associated with their deviation
In order to correctly assess the value of the parameters of protein fractions in a biochemical blood test, it is necessary to know the range of values at which the content of protein fractions in the blood will be considered normal. The second thing you need to know to assess the state of health is what pathologies can cause a change in the level of protein compounds.
Protein fractions content norms
Protein for a person under adulthood (under 21) is a valuable building material that the body uses to grow the body. After growing up, the balance of proteins becomes more stable and stable - any deviation from the norm will be a signal that pathological processes are taking place in the body. In the table of normal values for protein fractions, you can find the norms for adult men and women in the age range from 22 to 75 years.
| Protein fractions / gender | Age and years | |||
| 22-34 | 35-59 | 60-74 | 75 and older | |
| Men | ||||
| Albumin | 57,3-58,5 | 55,0-57,4 | 51,2-56,8 | 49,9-61,7 |
| Globulins | 41,5-42,7 | 42,6-45,0 | 43,2-48,8 | 38,3-51,1 |
| Alpha 1 -globulins | 5,2-5.5 | 4,6-5,6 | 5,3-6,3 | 3,0-5,4 |
| Alpha 2 -globulins | 6,1-7,5 | 7,7-8,9 | 7,4-10,4 | 5,6-11,0 |
| 8,2-10,6 | 12,6-14,2 | 11,2-13,6 | 11,1-12,7 | |
| 20,3-20.5 | 14.9-18,9 | 16,3-19,7 | 19,8-20.6 | |
| Women | ||||
| Albumin | 58,3-61,8 | 55.1-57,5 | 53,0-56,0 | 48.8-54,6 |
| Globulins | 38,3-41,8 | 42,5-44,9 | 43,9-46,9 | 45,7-51,5 |
| Alpha 1 -globulins | 3,9-4,7 | 4,1-5,1 | 5,3-6,1 | 4,5-6,6 |
| Alpha 2 -globulins | 6,7-7,9 | 7,5-8,7 | 9,0-10,6 | 8,0-11,0 |
| 9,4-10,6 | 11,3-12,7 | 11,6-13.6 | 11,5-14,1 | |
| 16,5-19,3 | 17,9-20,0 | 16,7-18,1 | 18,8-20,5 | |
Possible pathological conditions associated with deviations in the norms of protein fractions
Albumin is a protein that regulates colloid-osmotic balance. If it is not enough, the body will suffer from dehydration, if a lot - from puffiness.
Globulins are proteins that take part in the work of the immune system, their presence or absence will be a marker of the quality of the work of human immunity. In more detail about the pathological conditions associated with changes in the norm of the content of albumin and globulins, in the table below.
| Level | Albumin | Globulins |
| Promoted |
|
A-globulins:
B- globulins:
Υ- globulins:
|
| Reduced |
|
|
A decrease in the level of fibrinogen in the blood below the indicated values will be evidence of protein starvation of the human body. The increase is possibly due to the fact that the patient has experienced a severe burn or mechanical injury, suffers from an infectious disease, has internal sepsis, suffers from liver pathology.
Blood consists of a liquid part and corpuscles - blood cells. If you release the blood from the vessel into a dry test tube, then after a few minutes a dark red clot consisting of fibrin threads will form in it. The light yellow liquid above the clot is serum.
If the blood is mixed with a preservative solution and allowed to settle or subjected to centrifugation, then it will be divided into two main layers: the lower - red - a precipitate of formed elements (erythrocytes, leukocytes, platelets) and the upper - a transparent yellowish liquid - plasma. Serum differs from plasma in the absence of fibrinogen protein in it, which has passed into the blood clot.
Blood consists of 55% plasma and 45% of the corpuscles that are suspended in it.
Plasma is a complex biological medium containing 92% water, 7% protein and 1% fats, carbohydrates and mineral salts.
Plasma (serum) proteins of blood are high-molecular nitrogen-containing compounds. They have a complex structure, they include more than 20 amino acids. The latter got their name due to the presence of amine groups (NH2) and carboxyl (acid) groups (COOH). Amino acids have the properties of both acids and bases and can interact with various compounds.
Amino acids combine with each other to form large molecules of various proteins. The human body contains more than 100 thousand types of various protein molecules. According to their shape, they can be divided into fibrillar and globular.
Fibrillar proteins are elongated, filamentous; the length of the molecules is tens and hundreds of times their diameter. Globular protein molecules have the shape of a ball (lump), their length exceeds the diameter by no more than 3-10 times. There are also transitional forms.
Proteins include carbon (50.6-54.6%), oxygen (21.5-23.5%), hydrogen (6.5-7.3%), nitrogen (15-16%). In addition, proteins contain small amounts of sulfur, phosphorus, iron, copper and some other elements.
The chemical properties of proteins are in many ways similar to amino acids. A protein molecule, like an amino acid molecule, contains at least one free amino group and one carboxyl group.
Since a protein molecule contains a huge number of amino acids, there are a lot of such "free groups". Due to the properties of acids and bases, proteins can enter into a wide variety of chemical reactions with a wide variety of substances, performing their many functions in the body.
Proteins are conventionally divided into simple and complex. Proteins are called simple if they consist only of amino acids. These include protamine, histones, albumins, globulins and a number of others.
During the breakdown of complex proteins, along with amino acids, other compounds are formed: nucleic acids, phosphoric acid, carbohydrates, etc. groups.
Proteins are able to give or receive an electrical charge by becoming positively or negatively charged. If this happens at the same time, the protein molecule becomes electrically neutral.
The physicochemical properties of proteins determine their hydrophilicity - the ability to retain water, creating a colloidal solution. One acid group (COOH) is able to bind four, and amine (NH2) - three water molecules.
Each protein molecule is surrounded by a fairly dense water membrane of its own, firmly fixed on its surface. The force with which plasma proteins attract water to themselves is called colloid osmotic pressure, or oncotic pressure. It is equal to 23-28 mm Hg. Art.
With a decrease in the amount of proteins or a decrease in their hydrophilicity, an excess of "free" water is formed in the plasma, the hydrostatic pressure in the smallest vessels (capillaries) rises, and water begins to seep through the walls of the capillaries into the tissue. Oncotic (i.e., depending on the amount and properties of proteins) edema is formed. The occurrence of edema is associated with many other reasons.
In addition to active participation in water metabolism, blood plasma proteins also perform a number of important functions. They are involved in the blood clotting process.
Possessing many polar dissociating side chains, proteins are able to bind and transport various biological substances. Being one of the most important buffering systems of the blood, proteins maintain the constancy of homeostasis - the acid-base state (CBS) of the blood. Plasma proteins protect the body from the penetration of foreign elements, including foreign proteins.
In clinical practice, the total protein content in blood plasma and its fraction is determined.
The total amount of protein in the blood plasma is 65-85 g / l. In serum, protein is 2-4 g / l less than in plasma due to the absence of fibrinogen.
The total amount of protein can be decreased (hypoproteinemia) or increased (hyperproteinemia).
Hypoproteinemia occurs due to:
- insufficient intake of protein in the body;
- increased protein loss;
- protein formation disorders.
Insufficient intake of protein can be the result of prolonged fasting, a protein-free diet, and disturbances in the activity of the gastrointestinal tract. A significant loss of protein occurs in acute and chronic bleeding, malignant neoplasms.
Severe hypoproteinemia is a constant symptom of nephrotic syndrome, which is observed in many kidney diseases and is associated with the excretion of large amounts of protein in the urine.
Violation of protein formation is possible with insufficient liver function (hepatitis, cirrhosis, liver dystrophy).
Hyperproteinemia develops as a result of dehydration (dehydration) - the loss of part of the intravascular fluid. This happens when the body overheats, extensive burns, severe injuries, and certain diseases (cholera). Hyperproteinemia is observed in myeloma - severe suffering with the proliferation of plasma cells that produce paraproteins.
The composition of blood plasma proteins is extremely diverse. Modern research methods have identified more than 100 different plasma proteins, most of them are isolated in pure form and characterized.
The simplest proteins - albumin, globulins and fibrinogen - are found in plasma in large quantities, the rest are in negligible amounts.
Differences in proteins in amino acid composition, physicochemical properties made it possible to divide them into separate fractions with specific biological properties.
The separation can be carried out most accurately in an electric field during electrophoresis. The method is based on the fact that proteins with different electrical charges move at different speeds.
Plasma protein electrophoresis was first carried out by the Swedish scientist A. Tizelius (1930).
In the blood plasma of a healthy person, during electrophoresis on paper, five fractions can be detected.
When using other media (agar gel, polyacrylamide gel) or immunoelectrophoresis, more fractions can be obtained.
Albumin makes up the majority of plasma proteins. They retain water well, they account for up to 80% of the colloidal osmotic pressure of the blood.
Hypoalbuminemia (a lowered content of albumin in the blood plasma) occurs due to the same reasons as a decrease in the total amount of protein (low intake from food, large losses of protein, impaired synthesis, increased breakdown). Hypoalbuminemia causes a decrease in oncotic blood pressure, which leads to edema. The hydrophilicity of proteins is reduced by various toxic substances, alcohol.
Hyperalbuminemia occurs when the body is dehydrated.
Globulins. An increase in the content of alpha globulins is observed during inflammatory processes, stress effects on the body (trauma, burns, myocardial infarction, etc.).
These are proteins of the so-called acute phase. The degree of increase in alpha globulins reflects the intensity of the process.
The predominant increase in alpha-2-globulins is observed in acute purulent diseases, involvement of connective tissue in the pathological process (rheumatism, systemic lupus erythematosus, etc.).
A decrease in alpha globulins is noted when their synthesis is inhibited in the liver, hypothyroidism is a reduced function of the thyroid gland.
Beta globulins. This fraction contains lipoproteins, so the amount of beta-globulins increases with hyperlipoproteinemia. This is observed in atherosclerosis, diabetes mellitus, hypothyroidism, nephrotic syndrome.
Significant hypergammaglobulinemia is characteristic of chronic active hepatitis, liver cirrhosis.
In some diseases (myeloma, blood diseases, malignant neoplasms), special pathological proteins appear - paraproteins - immunoglobulins, devoid of the properties of antibodies. In these cases, hypergammaglobulinemia is also observed.
A decrease in gamma globulins is observed in diseases and conditions associated with exhaustion, suppression of the immune system (chronic inflammatory processes, allergies, terminal malignant diseases, long-term therapy with steroid hormones, AIDS).
Protein fractions- the quantitative ratio of the fractions of the total protein of blood serum: albumin, α-1-globulins, α-2-globulins, β-globulins and β-globulins.
Albumin fraction
homogeneous, normally it is 50-65% of the total amount of protein.
Globulin fractions are more heterogeneous in composition.
Fraction? -1-globulins includes alpha-1-antitrypsin (the main component of this fraction) - an inhibitor of proteolytic enzymes, alpha-1-acid glycoprotein (orosomucoid) - has a wide range of functions, promotes fibrillogenesis in the inflammation zone, alpha-1-lipoproteins (function - participation in transport of lipids), prothrombin and transport proteins: thyroxin-binding globulin, trancortin (function - binding and transport of cortisol and thyroxine, respectively).
Fraction? -2-globulins predominantly includes proteins of the acute phase - alpha-2 macroglobulin, haptoglobin, ceruloplasmin, as well as apolipoprotein B. Alpha-2-macroglobulin, which is the main component of the fraction, is involved in the development of infectious and inflammatory reactions. Haptoglobin is a glycoprotein that forms a complex with hemoglobin released from erythrocytes during intravascular hemolysis. Ceruloplasmin specifically binds copper ions, and is also an oxidase of ascorbic acid, adrenaline, dioxyphenylalanine (DOPA), and is capable of inactivating free radicals. Alpha lipoproteins are involved in lipid transport.
Fraction of? -Globulins contains transferrin (the main plasma protein - iron carrier), hemopexin (binds gem / methem, as a result of which prevents its excretion by the kidneys and the loss of iron), complement components (which take part in immune reactions), beta-lipoproteins (take part in the transport of cholesterol and phospholipids ) and some of the immunoglobulins.
Fraction of? -Globulins consists of immunoglobulins (according to the order of quantitative decrease - IgG, IgA, IgM, IgE). Functionally, immunoglobulins are antibodies that confer humoral immunity.
A change in the ratio of protein fractions in blood plasma is observed in many diseases with a normal content of total protein (dysproteinemia). Dysproteinemias are more common than changes in total protein. When observed in dynamics, they can characterize the stage of the disease, its duration, the effectiveness of the treatment measures being carried out.
Typical variants of shifts in the content of protein fractions.
The acute phase response (changes associated with inflammation and tissue necrosis) is an increase in the content of α-1- and β-2-globulins. It is observed in acute viral infection, acute pneumonia, acute bronchitis, acute pyelonephritis, myocardial infarction, trauma (including surgical), neoplasms.
Chronic inflammation - an increase in the content of β-globulins (rheumatoid arthritis, chronic hepatitis).
Nephrotic syndrome - an increase in the concentration of β-2-globulins in the blood (occurs due to the accumulation of alpha-2-macroglobulin against the background of the loss of albumin and other proteins during filtration in the renal glomeruli).
Liver cirrhosis is a significant increase in the gamma fraction proteins.
Indications for the purpose of the analysis - protein fractions:
- Acute and chronic inflammatory diseases (infections, diffuse connective tissue diseases, collagenoses, autoimmune diseases).
- Suspected multiple myeloma and other monoclonal gammopathies.
- Eating disorders and malabsorption syndrome.
- Screening examinations.
Preparation for research: taking blood on an empty stomach.
Material for research: blood serum.
Units:% (percent).
Reference values of protein fractions (norm for adults):
albumin 52 - 65%
? 1-globulins 2.5 - 5%
? 2-globulins 6 - 11%
β-globulins 8 - 14%
β-globulins 15 - 22%
1. Eating disorders. 2. Syndrome of malabsorption. 3. Diseases of the liver and kidneys. 4. Tumors. 5. Collagenosis. 6. Burns. 7. overhydration. 8. Bleeding. 9. Analbuminemia. 10. Pregnancy. 11. Severe inflammatory diseases.
Fraction of? -1-globulins.
1. Hereditary deficiency of alpha-1-antitrypsin. 2. Deficiency of alpha-1-lipoprotein.
Fraction of? -2-globulins.
1. Decrease in alpha-2-macroglobulin (pancreatitis, burns, trauma). 2. Decreased haptoglobin (hemolysis of various etiologies, pacreatitis, sarcoidosis).
Fraction of β-globulins.
1. Hypobetalipoproteinemia. 2. IgA deficiency.
Fraction of? -Globulins
1. Immunodeficiency states. 2. Taking glucocorticoids. 3. Plasmapheresis. 4. Pregnancy.
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I am very grateful to the people who work here for the kindness and warmth that they radiate, for the attitude that is so dear in our life, and right now. Many thanks to the doctors and nurses, all the staff. Here you feel calm and confident that everything will be fine with you!
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I sincerely express my gratitude to the entire staff of the clinic for the warm professional attitude towards the patient, for the complete and, most importantly for a pensioner, free treatment that gives a positive result (for osteoporosis). Thank you so much for the advice and important recommendations. I wish you all health, creative success in difficult medical work, all the best!
I am a healthcare professional with 17 years of experience. I work in the Central Regional Hospital of Verkhnedneprovsk. Until today in private ...
I am a healthcare professional with 17 years of experience. I work in the Central Regional Hospital of Verkhnedneprovsk. Until today, I have not been to private clinics and I really regret, after that, how I visited your clinic. This is the first time I have encountered such an attentive and professional attitude to my work. And the very atmosphere in the Clinic gives an excellent mood and the belief that all diseases are curable. Many thanks to Yu.N. Kulikovich. for the fact that he created such a Clinic with an excellent team.
In biochemical analysis, blood protein fractions reflect the state of protein metabolism.
Such a diagnosis is important for many diseases, so it is worthwhile to figure out what protein fractions are and what values are considered the norm.
Human blood plasma includes about a hundred different protein components (fractions). Most of them (up to 90%) are albumin, immunoglobulins, lipoproteins, fibrinogen.
The remainder includes other protein components present in plasma in small amounts.
Serum contains about 7% of all proteins, and their concentration reaches 60 - 80 g / l. The value of blood fractions is enormous.
Proteins provide the ideal acid-base balance of the blood, are responsible for the transport of substances, and control the viscosity of the blood. Proteins play a critical role in the circulation of blood through the vessels.
Basically, the protein fractions of the blood are produced by the liver (fibrinogen, albumin, some of the globulins). The rest of the globulins (immunoglobulins) are synthesized by the bone marrow and lymph RES cells.
The composition of the total protein of blood plasma includes albumins and globulins, which are in the established qualitative and quantitative proportion. In accordance with the research method, different amounts and types of protein fractions are isolated.
A blood test for protein fractions is most often carried out by electrophoretic fractionation. There are several types of electrophoresis, depending on the supporting environment.
So, when analyzed on film or gel, the following protein fractions of blood plasma are released: albumin (55 - 65%), α 1 -globulin (2 - 4%), α 2 -globulin (6 - 12%), β-globulin (8 - 12%), γ-globulin (12 - 22%).
The essence of the method is to assess the intensity of the bands of fractions in the total amount of protein. Protein fractions are presented in the form of bands of different widths and specific locations.
In clinical diagnostic laboratories, such a study is most often carried out.
A greater number of blood protein fractions are detected when using other media for electrophoretic research.
For example, a starch gel assay can isolate up to 20 protein fractions. In the course of modern examinations (radial immunodiffusion, immunoelectrophoresis, etc.), many individual proteins are found in the composition of globulin fractions.
In some pathologies, during electrophoretic research, the ratio of protein fractions changes in comparison with normal values. Such changes are called dysproteinemia.
Regardless of the presence of standard deviations in such analyzes, which often make it possible to confidently diagnose a pathology, usually the result of protein electrophoresis is not accepted as an unambiguous basis for the diagnosis and selection of a treatment regimen.
Therefore, the interpretation of the analysis is carried out in conjunction with other additional clinical and laboratory studies.
Fractions of albumin and globulins
Albumin is a simple water-soluble protein. The most famous type of albumin is serum albumin. The fraction is produced by the liver and makes up about 55% of all proteins contained in blood plasma.
Normal serum albumin levels in adults are between 35 and 50 g / L. For children under three years of age, normal values are between 25 and 55 g / l.
Albumin is produced by the liver and is dependent on amino acids. The main functions of the protein are considered to be the maintenance of plasma oncotic pressure and control of the BCC.
In addition, albumin, in conjunction with bilirubin, cholesterol, acids and other substances, participates in the exchange of minerals and hormones.
Fraction controls the free substance content of the non-protein bound fractions. This function of albumin allows it to be included in the detoxification process of the body.
Globulins are protein fractions of blood serum, which have a higher molecular weight and lower solubility in water, in contrast to albumin. The fractions are produced by the liver and the immune system.
Alpha1-globulins (prothrombin, transcortin, etc.) are responsible for the transport of cholesterol, cortisol, progesterone and other substances.
In addition, fractions are involved in the process of blood clotting (second phase). The normal content of alpha1-globulins in the blood serum is 3.5 to 6.5% (1 to 3 g / l).
At the same time, in children, the concentration of fractions of blood plasma proteins is slightly different: up to 6 months, values from 3.2 to 11.7% are considered the norm, with age, the upper limit drops and by 7 years it reaches the norm in adults.
Alpha2-globulins (antithrombin, vitamin D, binding protein, etc.) transport copper ions, retinol, calciferol.
The normal value of protein fractions in blood plasma in adults is in the range of 9 - 15% (from 6 to 10 g / l). In children under 18 years of age, a concentration of 10.6 to 13% is considered the norm.
Beta globulins (transferrin, fibrinogen, protein binding globulin, etc.) are responsible for the transport of cholesterol, iron ions, vitamin B 12, testosterone.
Beta globulins are involved in the first phase of the blood clotting process. In adults, the accepted norm for the concentration of fractions in plasma is from 8 to 18% (from 7 to 11 g / l). For children, a decrease in the level of protein in the blood to 4.8 - 7.9% is characteristic.
Gamma globulins (IgA, IgG, IgM, IgD, IgE) are antibodies and B-lymphocyte receptors that provide humoral immunity.
The normal value for adults is the concentration of gamma globulins in the blood from 15 to 25% (from 8 to 16 g / l). In children, a decrease in the level of protein fractions up to 3.5% (under the age of six months) and up to 9.8% (under the age of 18) is permissible.
What does deviation from the norm mean?
The study of protein fractions is important in the diagnosis of many diseases. Lack or excess of one type of protein disrupts the balance of blood plasma. In laboratories, there are 10 types of electrophoregrams that correspond to certain pathologies.
The first type is acute inflammation. These pathologies (pneumonia, pulmonary tuberculosis, sepsis, myocardial infarction) are characterized by a significant decrease in the level of albumin and an increase in the concentration of alpha1-, alpha2- and gamma-globulins.
The second type of electrophoretogram is chronic inflammation (for example, endocarditis, cholecystitis, and cystitis). In the analysis, a decrease in the level of albumin and a significant increase in the number of alpha2 and gamma globulins will be noticeable. Alpha1 and beta globulin levels will remain within normal limits.
The third type is responsible for violations of the renal filter (albumin and gamma globulin levels fall against the background of an increase in the concentration of alpha2 and beta globulins).
The fourth type is the most striking marker of the presence of malignant tumors and metastatic neoplasms.
With such a pathology, the analysis demonstrates a noticeable decrease in the level of albumin and a simultaneous increase in all globulin components of the protein. The location of the primary tumor does not affect the analysis parameters.
The fifth and sixth types indicate the presence of hepatitis, liver necrosis and some forms of polyarthritis. Against the background of a decrease in the concentration of albumin, an increase in gamma globulin and slight deviations from the norm of beta globulin are noticeable.
The seventh type of proteinogram signals the development of jaundice of various origins. The fall in albumin levels occurs with a simultaneous increase in the number of alpha2-, beta- and gamma-globulins.
The eighth, ninth and tenth types are responsible for myeloma of various origins. With a decrease in the concentration of albumin, an increase in globulin indicators is noted (for each type it is different).
Decoding of proteinogram indicators is carried out only by a specialist. Many features of the interpretation of the analysis, depending on the patient's condition and data from other examinations, do not allow the use of electrophoretogram as a direct diagnosis.
An analysis of the protein composition of the blood is prescribed for inflammatory processes in an acute or chronic form (any infections, pathologies of the immune system, collagenoses, etc.).
Plasma examination is performed in patients with suspected multiple myeloma and various paraproteinemias.
Metabolic disorders with malabsorption syndrome are a direct indication for analysis. Pregnant women donate blood for protein composition in a complex of screening diagnostics.
Demonstrates the ratio of plasma protein components. If the balance of the number of fractions is disturbed, then the patient is often diagnosed with an inflammatory process or disease in an acute or chronic form.
However, the interpretation of the research results should occur in conjunction with the indicators of other examinations and cannot be the only basis for the diagnosis and selection of the treatment regimen.
The human body has special systems that carry out continuous communication between organs and tissues and the exchange of waste products with the environment. One of these systems, along with interstitial fluid and lymph, is blood.
The functions of blood are as follows.
Nutrition of tissues and excretion of metabolic products.
Respiration of tissues and maintenance of acid-base balance and water-mineral balance.
Transport of hormones and other metabolites.
Protection from alien agents.
Regulation of body temperature by redistributing heat in the body.
Cellular elements of blood are in a liquid medium- blood plasma.
If freshly taken blood is left in a glass container at room temperature (20 ° C), then after a while a blood clot (thrombus) will form, after the formation of which a yellow liquid will remain - blood serum. It differs from blood plasma in that it does not contain fibrinogen and some proteins (factors) of the blood coagulation system. At the heart of blood coagulation is the conversion of fibrinogen into insoluble fibrin. Erythrocytes become entangled in fibrin filaments. Fibrin filaments can be obtained by long-term stirring of freshly taken blood, winding the resulting fibrin onto a stick. This way you can get defibrinated blood.
To obtain whole blood suitable for transfusion to a patient, capable of being stored for a long time, anticoagulants (substances that prevent blood clotting) must be added to the blood collection container.
The mass of blood in the vessels of a person is approximately 20% of the body weight. 55% of the blood mass is plasma, the rest is formed by blood plasma elements (erythrocytes, leukocytes, lymphocytes, platelets).
Plasma composition:
90% water;
6-8% - proteins;
2% - organic non-protein compounds;
1% - inorganic salts.
Protein components of blood plasma.
The salting-out method can be used to obtain three fractions of blood plasma proteins: albumins, globulins, fibrinogen. Electrophoresis on paper separates blood plasma proteins into 6 fractions.
Albumin - 54-62 %.
Globulins: 1-globulins 2.5-5%.
v2 globulins 8,5-10 %.
globulins 12-15 %.
globulins 15,5-21 %..
fibrinogen (remains at the start)- from 2 to 4%
Modern methods make it possible to obtain over 60 individual blood plasma proteins.
The quantitative ratios between protein fractions are constant in a healthy person. Sometimes the quantitative relationships between different fractions of blood plasma are violated. This phenomenon is called dysproteinemia. It happens that the content of total plasma protein is not disturbed.
with prolonged fasting;
when there is kidney pathology (loss of protein in the urine).
Rarely, but sometimes hyperproteinemia occurs - an increase in the plasma protein content is higher than 80 g / l. This phenomenon is typical for conditions in which there is significant loss of fluid by the body: indomitable vomiting, profuse diarrhea (in some severe infectious diseases: cholera, severe dysentery).
Characterization of individual protein fractions.
Albumin- simple low molecular weight hydrophilic proteins. The albumin molecule contains 600 amino acids. Molecular weight 67 kDa. Albumin, like most other blood plasma proteins, is synthesized in the liver. About 40% of albumin is in the blood plasma, the rest is in the interstitial fluid and in the lymph.
Albumin functions.
They are determined by their high hydrophilicity and high concentration in blood plasma.
Maintenance of oncotic blood plasma pressure. Therefore, with a decrease in the content of albumin in the plasma, the oncotic pressure drops, and the fluid leaves the bloodstream into the tissues. "Hungry" edema develops. Albumin provides about 80% of the plasma oncotic pressure. It is the albumin that is easily lost in the urine in kidney disease. Therefore, they play an important role in the drop in oncotic pressure in such diseases, which leads to the development of "renal" edema.
Albumin is a reserve of free amino acids in the body, formed as a result of the proteolytic cleavage of these proteins.
Transport function. Albumin transports many substances in the blood, especially those that are poorly soluble in water: free fatty acids, fat-soluble vitamins, steroids, and some ions (Ca2 +, Mg2 +). For the binding of calcium in the albumin molecule there are special calcium-binding centers. In a complex with albumin, many drugs are transported, for example, acetylsalicylic acid, penicillin.
Globulins.
Unlike albumin, globulins are not water-soluble, but soluble in weak saline solutions.
1-globulins
This fraction includes a variety of proteins. 1-globulins have high hydrophilicity and low molecular weight - therefore, with kidney pathology, they are easily lost in the urine. However, their loss does not significantly affect oncotic blood pressure, because their content in blood plasma is low.
Functions of v1-globulins.
Transport. They transport lipids, while forming complexes with them - lipoproteins. Among the proteins of this fraction there is a special protein intended for the transport of the thyroid hormone thyroxine - thyroxine-binding protein.
Participation in the functioning of the blood coagulation system and the complement system - this fraction also contains some blood coagulation factors and components of the complement system.
Regulatory function. Some proteins of the 1-globulin fraction are endogenous inhibitors of proteolytic enzymes. The highest plasma concentration of 1-antitrypsin. Its content in plasma is from 2 to 4 g / l (very high), molecular weight - 58-59 kDa. Its main function is to inhibit elastase, an enzyme that hydrolyzes elastin (one of the main proteins of connective tissue). 1-antitrypsin is also an inhibitor of proteases: thrombin, plasmin, trypsin, chymotrypsin and some enzymes of the blood coagulation system. The amount of this protein increases in inflammatory diseases, during the processes of cellular decay, decreases in severe liver diseases. This decrease is the result of a violation of the synthesis of 1-antitrypsin, and it is associated with excessive cleavage of elastin. There is a congenital deficiency (1-antitrypsin. It is believed that a lack of this protein contributes to the transition of acute diseases into chronic ones.
The fraction of 1-globulins also includes 1-antichymotrypsin. It inhibits chymotrypsin and some blood cell proteinases.
2-globulins
High molecular weight proteins. This fraction contains regulatory proteins, blood coagulation factors, components of the complement system, transport proteins. This includes ceruloplasmin. This protein has 8 copper binding sites. It is a carrier of copper, and also ensures the constancy of copper content in various tissues, especially in the liver. With a hereditary disease - Wilson's disease - the level of ceruloplasmin decreases. As a result, the concentration of copper in the brain and liver increases. This is manifested by the development of neurological symptoms, as well as cirrhosis of the liver.
Haptoglobins.
Complexes of hemoglobin with haptoglobin are destroyed by cells of the reticuloendothelial system (cells of the mononuclear phagocyte system), after which globin is split into amino acids, heme is destroyed to bilirubin and excreted by bile, and iron remains in the body and can be reused. This fraction also includes 2-macroglobulin. The molecular weight of this protein is 720 kDa, the concentration in blood plasma is 1.5-3 g / l. It is an endogenous inhibitor of proteinases of all classes, and also binds the hormone insulin. The half-life of 2-macroglobulin is very short - 5 minutes. This is a universal "cleaner" of blood, complexes "2-macroglobulin-enzyme" are able to absorb immune peptides, for example, interleukins, growth factors, tumor necrosis factor, and remove them from the bloodstream. C 1 -inhibitor - a glycoprotein, is the main regulatory link in the classical pathway of complement activation (CPA), is able to inhibit plasmin, kallikrein. With a lack of C 1 -inhibitor, angioedema develops.
Globulins
This fraction includes some proteins of the blood coagulation system and the vast majority of components of the complement activation system (from C 2 to C 7).
The basis of the faction-globulins make up Low Density Lipoproteins (LDL) (For more information on lipoproteins: see the lectures "Lipid Metabolism").
C-reactive protein. Contained in the blood of healthy people in very low concentrations, less than 10 mg / l. Its function is unknown. The concentration of C-reactive protein increases significantly in acute inflammatory diseases. Therefore, C-reactive protein is called the "acute phase" protein (acute phase proteins also include -1-antitrypsin, haptoglobin).
Gamma globulins
This fraction contains mainly antibodies- proteins synthesized in the lymphoid tissue and in the cells of the RES, as well as some components of the complement system.
Antibody function- protection of the body from foreign agents (bacteria, viruses, foreign proteins), which are called antigens.
The main classes of antibodies in the blood:
immunoglobulins G (IgG);
immunoglobulins M (IgM);
immunoglobulins A (IgA), which include IgD and IgE.
Only IgG and IgM are able to activate the complement system. C-reactive protein is also able to bind and activate the C1 component of complement, but this activation is counterproductive and leads to the accumulation of anaphylotoxins. The accumulated anaphylotoxins cause allergic reactions.
Cryoglobulins also belong to the group of gamma globulins. These are proteins that can precipitate when whey is cooled. Healthy people do not have them in serum. They appear in patients with rheumatoid arthritis and multiple myeloma.
Among the cryoglobulins, there is a protein called fibronectin. It is a high molecular weight glycoprotein (molecular weight 220 kDa). It is present in blood plasma and on the surface of many cells (macrophages, endothelial cells, platelets, fibroblasts).
Fibronectin functions:
ensures the interaction of cells with each other;
promotes platelet adhesion;
prevents metastasis of tumors.
Plasma fibronectin is an opsonin- enhances phagocytosis. Plays an important role in cleansing the blood from protein breakdown products, for example, collagen breakdown. Coming into contact with heparin, it participates in the regulation of blood coagulation processes. Currently, this protein is widely studied and used for diagnosis, especially in conditions accompanied by inhibition of the macrophage system (sepsis, etc.).
Interferon is a glycoprotein. Has a molecular weight of about 26 kDa. Possesses species specificity. It is produced in cells in response to the introduction of viruses into them. In a healthy person, its concentration in plasma is low. But with viral diseases, its concentration increases.
The structure of the immunoglobulin molecule.
Molecules of all classes of immunoglobulins have a similar structure. Let's analyze their structure using the example of an IgG molecule. These are complex proteins that are glycoproteins and have a quaternary structure.
The protein part of the immunoglobulin contains only 4 polypeptide chains: 2 identical light and 2 identical heavy chains. The molecular weight of the light chain is 23 kDa, and that of the heavy chain is from 53 to 75 kDa. With the help of disulfide (-S-S-) bonds (bridges), the heavy chains are interconnected and the light chains are also held near the heavy chains.
If an immunoglobulin solution is treated with the proteolytic enzyme papain, then the immunoglobulin molecule is hydrolyzed to form 2 variable regions and one constant part.
The light chain, starting from the N-end, and the same length of the H-chain form a variable region - Fab-fragment. The amino acid composition of the Fab fragment is very different for different immunoglobulins. The Fab fragment can bind to the corresponding antigen by weak linkages. It is this site that provides the specificity of the binding of the immunoglobulin to its antigen. Within the immunoglobulin molecule, an Fc-fragment is also isolated - a constant (identical) part of the molecule for all immunoglobulins. Formed by H-chains. There are sites that interact with the first component of the complement system (or with receptors on the surface of a certain type of cells). In addition, the Fc fragment sometimes allows the passage of the immunoglobulin across the biological membrane, for example, through the placenta. The interaction of the Fab fragment with its antigen leads to a significant change in the conformation of the entire immunoglobulin molecule. In this case, one or another site becomes available within the Fc-fragment. The interaction of this opened center with the first component of the complement system or with cell receptors, which leads to the formation of an immune complex "antigen-antibody".
The synthesis of immunoglobulins is significantly different from the synthesis of other proteins. Each of the L-chains is encoded by a group of 3 different genes, and the H-chain is encoded by four genes. Thus, a huge variety of the structure of antibodies, their specificity for various antigens is provided. The human body can potentially synthesize approximately 1 million different antibodies.
Fibrinogen.
It is a protein to which the action of the blood coagulation system is directed. When blood clots, fibrinogen is converted to fibrin, which is insoluble in water and falls out in the form of threads. These filaments entangle the formed elements of the blood and, thus, a blood clot (thrombus) is formed.
Proteins-enzymes of blood plasma
By function, proteins-enzymes of blood plasma are divided into:
actual plasma enzymes- perform specific metabolic functions in plasma. The actual plasma enzymes include such proteolytic systems as the complement system, the vascular tone regulation system, and some others;
enzymes that enter the plasma as a result of damage to an organ or tissue as a result of cell destruction. Usually do not perform a metabolic function in plasma. However, for medicine, it is of interest to determine the activity of some of them in blood plasma for diagnostic purposes (transaminases, lactate dehydrogenase, creatine phosphokinase, etc.).
Organic non-protein compounds of plasma are divided into two groups.
I group- nitrogen-containing non-protein components.
The composition of non-protein nitrogen in the blood includes nitrogen of intermediate and final metabolic products of simple and complex proteins.
Previously, non-protein nitrogen was called residual nitrogen (remains after precipitation of proteins):
urea nitrogen (50%);
amino acid nitrogen (25%);
low molecular weight peptides;
creatinine;
bilirubin;
some other nitrogen-containing substances.
In some kidney diseases, as well as in pathology accompanied by massive destruction of proteins (for example, severe burns), non-protein blood nitrogen may increase, i.e., azotemia is observed. However, it is not the total content of non-protein nitrogen in the blood that is most often violated, but the ratio between the individual components of non-protein nitrogen. Therefore, the nitrogen of individual components is now determined in the plasma.
The term "residual nitrogen" also includes low molecular weight peptides. Among the low molecular weight peptides, there are many peptides with high biological activity (for example, hormones of a peptide nature).
II group - nitrogen-free organic substances.
Nitrogen-free (do not contain nitrogen) organic substances in blood plasma include:
carbohydrates, lipids and products of their metabolism (glucose, PVC, lactate, ketone bodies, fatty acids, cholesterol and its esters, etc.);
mineral substances of shelter.
Blood cells and features of their metabolism
Red blood cells.
Main function- transport of gases: transfer of О 2 and СО 2. It is possible due to the high content of hemoglobin and the high activity of the enzyme carbonic anhydrase.
Mature erythrocytes do not have nuclei, ribosomes, mitochondria, lysosomes. Therefore, the exchange of erythrocytes has a number of features.
In mature erythrocytes, protein biosynthesis reactions do not take place.
Energy is generated only by glycolysis, the substrate is only glucose.
In erythrocytes, there are mechanisms for protecting hemoglobin from oxidation.
The GMP pathway of glucose breakdown, which gives NADPH 2, is actively proceeding.
There is a high concentration of glutathione, a peptide containing SH-groups.
Leukocytes.
Cells that perform protective functions- are capable of phagocytosis. There are many active proteases in leukocytes that break down foreign proteins. At the time of phagocytosis, the production of hydrogen peroxide increases and the activity of peroxidase increases, which contributes to the oxidation of foreign particles (antibacterial effect). Leukocytes are rich in intracellular low-specific proteinases - cathepsins, localized in lysosomes. Cathepsins are capable of almost total proteolysis of protein molecules. In the lysosomes of leukocytes, other enzymes are also contained in significant quantities: for example, ribonuclease and phosphatase.
Biology and genetics
Almost all plasma proteins, with the exception of albumin, are glycoproteins. Oligosaccharides attach to proteins, forming glycosidic bonds with the hydroxyl group of serine or threonine, or interacting with the carboxyl group of asparagine. The terminal residue of oligosaccharides in most cases is N-acetylneuraminic acid combined with galactose
The main protein fractions of blood plasma and their functions. The value of their definition for the diagnosis of diseases. Enzymodiagnostics.
The blood plasma contains 7% of all body proteins at a concentration of 60 - 80 g / l. Plasma proteins have many functions. One of them is to maintain osmotic pressure, as proteins bind water and keep it in the bloodstream. Plasma proteins form the most important buffer system of the blood and maintain the blood pH in the range of 7.37 - 7.43. Albumin, transthyretin, transcortin, transferrin and some other proteins perform a transport function. Plasma proteins determine the viscosity of the blood and, therefore, play an important role in the hemodynamics of the circulatory system. Plasma proteins are the body's reserve of amino acids. Immunoglobulins, proteins of the blood coagulation system, α1-antitrypsin and proteins of the complement system carry out a protective function. By electrophoresis on cellulose acetate or agarose gel, plasma proteins can be divided into albumin (55-65%), α1-globulins (2-4%), α2-globulins (6-12%), β-globulins (8-12%) and γ-globulins (12-22%). The use of other media for electrophoretic separation of proteins allows the detection of a larger number of fractions. For example, during electrophoresis in polyacrylamide or starch gels, 16-17 protein fractions are isolated in blood plasma. The method of immunoelectrophoresis, combining electrophoretic and immunological methods of analysis, makes it possible to separate blood plasma proteins into more than 30 fractions. Most whey proteins are synthesized in the liver, but some are also produced in other tissues. For example, γ-globulins are synthesized by B-lymphocytes, peptide hormones are mainly secreted by endocrine gland cells, and peptide hormone erythropoietin is secreted by kidney cells. Many plasma proteins, such as albumin, α1-antitrypsin, haptoglobin, trans-ferrin, ceruloplasmin, α2-macroglobulin, and immunoglobulins, are polymorphic.
Almost all plasma proteins, with the exception of albumin, are glycoproteins. Oligosaccharides attach to proteins, forming glycosidic bonds with the hydroxyl group of serine or threonine, or interacting with the carboxyl group of asparagine. The terminal residue of oligosaccharides in most cases is N-acetylneuraminic acid combined with galactose. The vascular endothelial enzyme neuraminidase hydrolyzes the bond between them, and galactose becomes available for specific receptors of hepatocytes. Through eudcytosis, "aged" proteins enter the liver cells, where they are destroyed. T 1/2 of blood plasma proteins ranges from several hours to several weeks. In a number of diseases, there is a change in the ratio of the distribution of protein fractions during electrophoresis in comparison with the norm. Such changes are called dysproteinemias, but their interpretation often has relative diagnostic value. For example, a decrease in albumin, α1- and γ-globulins, and an increase in α2- and β-globulins, characteristic of nephrotic syndrome, are also noted in some other diseases accompanied by loss of proteins. With a decrease in humoral immunity, a decrease in the fraction of γ-globulins indicates a decrease in the content of the main component of immunoglobulins - IgG, but does not reflect the dynamics of changes in IgA and IgM. The content of some proteins in the blood plasma can sharply increase in acute inflammatory processes and some other pathological conditions (trauma, burns, myocardial infarction). Such proteins are called proteins of the acute phase, since they take part in the development of the body's inflammatory response. The main inducer of the synthesis of most acute phase proteins in hepatocytes is the interleukin-1 polypeptide, which is released from mononuclear phagocytes. Acute phase proteins includeC-reactive protein, so called because it interacts with the C-polysaccharide of pneumococci, α1-antitrypsin, haptoglobin, acidic glycoprotein, fibrinogen. It is known that C-reactive protein can stimulate the complement system, and its concentration in the blood, for example, during an exacerbation of rheumatoid arthritis, can increase 30 times compared to the norm. Plasma protein α1-antitrypsin can inactivate some proteases released in the acute phase of inflammation.
Albumen. The concentration of albumin in the blood is 40-50 g / l. About 12 g of albumin is synthesized in the liver per day, T1 / 2 of this protein is about 20 days. Albumin consists of 585 amino acid residues, has 17 disulfide bonds and has a molecular weight of 69 kDa. The albumin molecule contains many dicarboxylic amino acids, therefore it can retain Ca2 +, Cu2 +, Zn2 + cations in the blood. About 40% of albumin is found in the blood and the remaining 60% in the intercellular fluid, but its concentration in the plasma is higher than in the intercellular fluid, since the volume of the latter exceeds the plasma volume by 4 times. Due to its relatively low molecular weight and high concentration, albumin provides up to 80% of the osmotic pressure of plasma. With hypoalbuminemia, the osmotic pressure of blood plasma decreases. This leads to an imbalance in the distribution of extracellular fluid between the vascular bed and the intercellular space. Clinically, this manifests itself as edema. The relative decrease in blood plasma volume is accompanied by a decrease in renal blood flow, which causes stimulation of the reninangiotensin aldrsterone system, which ensures the restoration of blood volume. However, with a lack of albumin, which must retain Na +, other cations and water, water goes into the intercellular space, increasing edema. Hypoalbuminemia can also be observed as a result of a decrease in the synthesis of albumin in liver diseases (cirrhosis), with an increase in capillary permeability, with protein losses due to extensive burns or catabolic conditions (severe sepsis, malignant neoplasms), with nephrotic syndrome, accompanied by albuminuria, and starvation. Circulatory disorders, characterized by a slowdown in blood flow, lead to an increase in the flow of albumin into the extracellular space and the appearance of edema. The rapid increase in capillary permeability is accompanied by a sharp decrease in blood volume, which leads to a drop in blood pressure and is clinically manifested as shock. Albumin is the most important transport protein. It transports free fatty acids, unconjugated bilirubin Ca2 +, Cu2 +, tryptophan, thyroxine, and triiodothyronine. Many drugs (aspirin, dicumarol, sulfonamides) bind to albumin in the blood. This fact must be taken into account in the treatment of diseases accompanied by hypoalbuminemia, since in these cases the concentration of the free drug in the blood increases. In addition, it should be remembered that some drugs can compete for binding sites in the albumin molecule with bilirubin and among themselves.
Transthyretin (prealbumin ) is called thyroxine-binding prealbumin.It is an acute phase protein... Transthyretin belongs to the albumin fraction, it has a tetrameric molecule. It is capable of attaching a retinol-binding protein in one binding site, and up to two molecules of thyroxine and triiodothyronine in the other.
The connection with these ligands occurs independently of each other. In the transport of the latter, transthyretin plays a significantly smaller role in comparison with thyroxine-binding globulin.
α1 - Antitrypsin belongs to α1-globulins. It inhibits a number of proteases, including the enzyme elastase, which is released from neutrophils and destroys the elastin of the alveoli of the lungs. With a deficiency of α1-antitrypsin, pulmonary emphysema and hepatitis can occur, leading to cirrhosis of the liver. There are several polymorphic forms of α1-antitrypsin, one of which is pathological. In people homozygous for two defective alleles of the antitrypsin gene, α1-antitrypsin is synthesized in the liver, which forms aggregates that destroy hepatocytes. This leads to a violation of the secretion of such a protein by hepatocytes and to a decrease in the content of α1-antitrypsin in the blood.
Haptoglobin makes up about a quarter of all α2-globulins. During intravascular hemolysis of erythrocytes, haptoglobin forms a complex with hemoglobin, which is destroyed in the RES cells. If free hemoglobin, which has a molecular weight of 65 kDa, can filter through the glomeruli or aggregate in them, then the hemoglobin-haptoglobin complex has too large a molecular weight (155 kDa) to pass through the glomeruli. Consequently, the formation of such a complex prevents the body from losing iron contained in hemoglobin. Determination of the content of haptoglobin is of diagnostic value, for example, a decrease in the concentration of haptoglobin in the blood is observed in hemolytic anemia. This is explained by the fact that at T1 / 2 of haptoglobin, which is 5 days, and T1 / 2 of the hemoglobin-haptoglobin complex (about 90 minutes), an increase in the supply of free hemoglobin into the blood during hemolysis of erythrocytes will cause a sharp decrease in the content of free haptoglobin in the blood. Haptoglobin include to proteins of the acute phase, its content in the blood rises in acute inflammatory diseases.
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Concentration in blood serum, g / l |
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Albumin |
Transthyretin |
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Albumen |
Maintenance of osmotic pressure, transport of fatty acids, bilirubin, bile acids, steroid hormones, drugs, inorganic ions, amino acid reserve |
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α1-Globulins |
α1-Antitrypsin |
Proteinase inhibitor |
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Cholesterol transport |
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Prothrombin |
Clotting factor II |
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Transcortin |
Transport of cortisol, corticosterone, progesterone |
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Acid α1-glycoprotein |
Progesterone transport |
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Thyroxine binding globulin |
Transport of thyroxine and triiodothyronine |
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α2-Globulins |
Ceruloplasmin |
Copper ion transport, oxidoreductase |
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Antithrombin III |
Plasma protease inhibitor |
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Haptoglobin |
Hemoglobin binding |
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α2-Macroglobulin |
Plasma proteinase inhibitor, zinc transport |
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Retinol-binding protein |
Retinol transport |
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Vitamin D binding protein |
Calciferol transport |
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β-globulins |
Cholesterol transport |
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Transferrin |
Iron ion transport |
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Fibrinogen |
Clotting factor I |
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Transcobalamin |
Vitamin B12 transport |
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Globulin binding protein |
Transport of testosterone and estradiol |
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C-reactive protein |
Complement activation |
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γ-Globulins |
Late antibodies |
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Antibodies that protect mucous membranes |
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Early antibodies |
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B-lymphocyte receptors |
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Enzymodiagnostics - methods for diagnosing diseases, pathological conditions and processes based on determining the activity of enzymes (enzymes) in biological fluids. A special group includes enzyme immunoassay diagnostic methods, consisting in the use of antibodies chemically bound to an enzyme to determine in liquids substances that form antigen-antibody complexes with these antibodies. The use of enzyme tests is an important criterion in recognizing congenital enzymopathies characterized by specific metabolic and vital disorders due to the absence or deficiency of one or another enzyme. Enzymes are specific high molecular weight protein molecules that are biological catalysts, i.e. accelerating chemical reactions in living organisms. The penetration of enzymes from cells into the extracellular fluid, and then into the blood, urine or other biological fluids is an extremely sensitive indicator of damage to plasma membranes or an increase in their permeability (for example, due to hypoxia, hypoglycemia, exposure to certain pharmacological substances, infectious agents, toxins). This circumstance underlies the diagnosis of damage to the cells of organs and tissues by the phenomenon of the accompanying hyperenzymemia, and the detected increase in the activity of the enzyme or its isoform may have a different degree of specificity for the damaged organ. The distribution of individual isoenzymes in tissues is more specific for a particular tissue than the total enzymatic activity; therefore, the study of some isoenzymes has become important for the early diagnosis of damage to individual organs and tissues. For example, the determination of the activity of creatine phosphokinase isoenzymes in the blood is widely used for the diagnosis of acute myocardial infarction., lactate dehydrogenase - for the diagnosis of liver and heart damage, acid phosphatase - and the recognition of prostate cancer The diagnostic value of enzyme tests is quite high; it depends both on the specificity of this type of hyperenzymemia for certain diseases, and on the degree of sensitivity of the test, i.e. the multiplicity of the increase in the activity of the enzyme in this disease relative to normal values. However, the timing of the test is of great importance. the appearance and duration of hyperenzymemia after organ damage are different and are determined by the ratio of the rate of entry of the enzyme into the bloodstream and the rate of its inactivation. In individual diseases, the reliability of their diagnosis can be increased by examining not one but several isoenzymes. So, for example, the reliability of the diagnosis of acute myocardial infarction increases if, at certain times, an increase in the activity of creatine phosphokinase, lactate dehydrogenase and aspartic aminotransferase is noted. The degree of detected hyperenzymemia objectively reflects the severity and prevalence of organ damage, which makes it possible to predict the course of the disease.
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Proteins - a group of the most complex and highly organized organic molecules in nature... They are represented by a huge number of species and subspecies, and each of them has its own function or set of functions. It is not surprising that a blood protein test provides a doctor with a wealth of useful information. The simplest analysis is the analysis for total protein, but it is not very informative: at best, you can tell from it whether everything is in order (and almost no one has everything in order). Therefore, an in-depth study is valuable: analysis for protein fractions in a biochemical blood test. What he really is?
As mentioned above, in a person's blood (as well as in a person himself) many different proteins can be found... The analysis for protein fractions of blood allows you to determine the level of the most valuable proteins for diagnostics: albumin, globulins and fibrinogen.
Albumen
60% by weight of all proteins circulating in the blood is albumin. Albumin is produced by the liver and its main functions are to maintain normal blood pressure and transport large insoluble molecules such as drug molecules.
In addition, albumin is a reserve protein: if the body for some reason does not have enough food, then albumin is consumed first.Globulins
Globulins (alternative name: C-reactive protein) are a class of molecules that are actively involved in the formation of immunity and immune response.
In their free time from fighting pathogens, globulins are moonlighting as transporters of cholesterol.
Alpha globulin
This type of globulin is responsible for the primary response to infection. It is divided into 2 types:
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Anna Ponyaeva. Graduated from the Nizhny Novgorod Medical Academy (2007-2014) and the Residency in Clinical and Laboratory Diagnostics (2014-2016).
- alpha globulin 1 inhibits unwanted chemical reactions at the site of inflammation;
- alpha globulin 2 forms primary threat recognition and primary immune response.
Human serum albumin
Albumin and globulins are the main groups of plasma proteins. Analysis of individual protein fractions serves as a marker of protein metabolism disorders, allows to identify various pathologies, monitor changes in diseases, and choose an effective treatment strategy.
Albumin (A) perform many tasks in the human body: maintain oncotic blood pressure, ensure the integrity of vascular barriers; transport fatty acids, hormones, vitamins; bind to derivatives of various substances, limiting their harmful effects on cells; interact with coagulation factors, serve as a source of amino acids.
Globulin structure
Globulins (G) are a heterogeneous group:
- α1-G: transfer lipids, acids, hormones; participate in coagulation processes, inhibit various enzymes.
- α2-G: bind hemoglobin and enzymes, transport vitamins and copper atoms, regulate coagulation processes.
- β-G: transport lipids and iron; bind to sex hormones, proteins and other elements.
- γ-G: predominantly immunoglobulins, the main function of which is to neutralize harmful agents that enter the body.
Standards for protein fractions
The analysis takes into account the albumin / globulin ratio
The analysis takes into account the ratio of fractions A / G, the norm of this value = 1: 2.
Reference values for the albumin fraction.
The norm for the fraction of globulins.
| Age | α1-G (g / l) | α2-G (g / l) | β-G (g / l) | γ-G (g / l) |
|---|---|---|---|---|
| 0 - 7 days | 1,2 - 4,2 | 6,8 - 11,2 | 4,5 - 6,7 | 3,5 - 8,5 |
| 7 days - 1 year | 1,24 - 4,3 | 7,1 - 11,5 | 4,6 - 6,9 | 3,3 - 8,8 |
| 1 year - 5 years | 2,0 - 4,6 | 7,0 - 13,0 | 4,8 - 8,5 | 5,2 - 10,2 |
| 5 - 8 years old | 2,0 - 4,2 | 8,0 - 11,1 | 5,3 - 8,1 | 5,3 - 11,8 |
| 8-11 years old | 2,2 - 3,9 | 7,5 - 10,3 | 4,9 - 7,1 | 6,0 - 12,2 |
| 11 - 21 years old | 2,3 - 5,3 | 7,3 - 10,5 | 6,0 - 9,0 | 7,3 - 14,3 |
| over 21 years old | 2,1 - 3,5 | 5,1 - 8,5 | 6,0 - 9,4 | 8,1 - 13,0 |
| ratio to total protein (%) | 2 - 5 | 7 - 13 | 8 - 15 | 12 - 22 |
Guideline values may vary from laboratory to laboratory.
Deviations from the norm: reasons for increasing and decreasing
Intestinal infections can cause dehydration
Increased albumin levels:
- dehydration,
- infectious infections,
- extensive burns and injuries.
Decrease in albumin levels:
In autoimmune diseases, gamma globulins increase
Increased level of globulins:
- α1-G: exacerbation of chronic diseases, damage to liver tissue;
- α2-G: acute inflammatory processes (kidney pathology, pneumonia, etc.);
- β-G: lipid metabolism disorders, liver, kidney, stomach diseases;
- γ-G: inflammation, infection, hepatitis, autoimmune diseases, malignant pathologies.
Decreased level of globulins:
- α1-G: deficiency of proteins of this fraction;
- α2-G: diabetes mellitus, hepatitis;
- β-G: decreased level of fi-proteins;
- γ-G: suppression of the immune system.
Indications for analysis
There are a number of indications for the purpose of the study.
The analysis is assigned in the following cases:
- As a comprehensive survey.
- In diseases associated with diffuse connective tissue damage.
- Infectious diseases in acute and chronic periods.
- Suspected malabsorption syndrome.
- With autoimmune pathologies.
- With diseases of the liver, kidneys.
- To differentiate puffiness.
- Identification of malignant processes.
Test preparation
Test preparation ensures reliable results
Correct preparation for analysis allows you to get correct results.
- The last meal should be completed 8 hours before the study, but the hunger period should be no more than 14 hours. It is recommended to drink clean water, excluding any drinks.
- Do not drink alcohol one day before blood withdrawal, smoking is limited one hour before the test.
- On the eve of the test, you should not overload the body emotionally and physically; it is better to postpone a trip to the gym.
- All other studies (X-ray, ultrasound) are carried out after the analysis.
- Blood sampling is done in the morning.
- The analysis result for protein fractions is influenced by hormonal drugs, including oral contraceptives, as well as cytostatic agents. If it is impossible to exclude their intake, it is necessary to provide a list of drugs to the doctor.
Methods for the determination of protein fractions
The study of protein fractions is carried out by several methods.
The following methods are used to separate proteins into fractions:
- Salting out. The technique is based on the ability of proteins to precipitate in the presence of salt solutions.
- Cohn's method. Separation into fractions at temperatures from -3 to -5 ° C with the interaction of different concentrations of ethanol.
- Immunological: immunoprecipitation, immunoelectrophoresis, radial immunodiffusion. The methods are based on the immune properties of protein fractions.
- Chromatography. Separation takes place in a specific adsorbent layer. The method includes: ion exchange, affinity, distribution and adsorption chromatography.
- Nitometric. Fractionation is carried out by breaking down the protein with sulfuric acid.
- Fluorometric. The method is based on the measurement of the fluorescence of a protein marked with fluorescemin.
The most popular techniques at present:
- Electrophoresis. The technique is based on the difference in the rate of protein mobility in an electric field.
- Colorimetry. The intensity of the light flux passing through the colored solution is measured.
Interpretation of results
The interpretation of the results is carried out by a specialist
The analysis can reveal a change in total plasma protein. In this case, it is necessary to investigate at the expense of which faction the change occurred.
Hyperproteinemia is an increase in total protein. If at the same time the number of γ-G is increased, the doctor may suspect an infectious infection. An increased concentration of β-G most often indicates pathological processes in the liver. Proteins of the acute phase belong to α-G, their growth indicates an intense inflammatory process.
Hypoproteinemia is a decrease in total protein levels. If the decrease occurs due to the α-G fractions, the presence of destructive processes in the liver and pancreas is suspected. The deficiency of the γ-G fraction is indicative, which is characteristic of the depletion of the immune system in chronic pathologies, malignant neoplasms. A decrease in β-G may indicate an unbalanced diet with diets, pathologies of the gastrointestinal tract.
Paraproteinemia is the formation of non-standard proteins (paraproteins), which will increase the γ-G fraction and will indicate a number of oncological diseases, autoimmune pathologies.
Defectoproteinemia is the absence of any protein, most often as a result of a violation of protein synthesis. For example, the α2-G fraction can be reduced due to the lack of ceruloplasmin, as a consequence of the presence of Wilson's disease.
Liver disease can lead to dysproteinemia
Dysproteinemia is a violation of the quantitative ratio between protein fractions. At the same time, the level of total protein remains normal. For example, in liver diseases, albumin decreases, globulins (due to γ-G) increase.
Thus, the result of the analysis must be considered in a complex, taking into account the correlation of the values of individual fractions.
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