3 Different Types Of Proteins And Their Functions – Blood plasma is a pale, straw-colored fluid composed of water, proteins, hormones, and nutrients. In other words, blood plasma is blood without blood cells, of which 92% of plasma is water, 7% belongs to plasma proteins, and >1% is regulatory proteins and other solutes.

Plasma proteins are the carriers of many blood functions. The purpose of this article is to help you understand its structure and function under physiological and pathological conditions.

3 Different Types Of Proteins And Their Functions

3 Different Types Of Proteins And Their Functions

Blood plasma is a liquid in which the formed elements are suspended. It floats at the top of the tube, separated from the denser elements, the erythrocytes, which are separated by a white coat of leukocytes and platelets. Hematocrit is the percentage of erythrocytes in the total sample.

Proteins And Their Functions

Although a small percentage (7%) belongs to plasma proteins, they perform many blood functions: coagulation process, regulation of acid-base balance, protection against pathogens, transport of nutrients and hormones, waste removal, regulation of osmotic pressure, control of erythrocyte sedimentation rate, etc. .

Plasma proteins can be separated by one method known as electrophoresis, where they migrate as separate fractions based on their size and electrical charge. Three plasma protein fractions are visible on the electrophoresis interface: albumins, globulins, and fibrinogen. Below, we review these individual plasma protein components, including their structure and biological function.

Albumin is the most common protein content of plasma and normally accounts for about 54% of total plasma protein content. It is produced by the liver and serves as a transporter of fatty acids and hydrophobic steroid hormones. In addition, albumin is the most important contributor to blood osmotic pressure: keeping water in blood vessels helps maintain blood volume and blood pressure.

Next we have the globulin fraction, a heterogeneous group containing alpha, beta, and gamma globulins. Alpha and beta globulins transport iron, lipids, and fat-soluble vitamins such as K, A, D, and E. Gamma globulins are central to humoral immunity and are called antibodies or immunoglobulins. Unlike alpha and beta globulins, which are produced in the liver, immunoglobulins are produced by transformed B cells known as plasma cells.

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Fibrinogen is the least abundant plasma protein, accounting for 7% of the total plasma protein volume. Fibrinogen, a liver product, is the first factor in the coagulation cascade.

Plasma proteins involved in hormone transport include corticosteroid-binding globulin, thyroxine-binding globulin, insulin-like growth factor-binding protein 3, sex hormone-binding globulin, and alpha-fetoprotein, to name a few.

Albumin is a single long polypeptide chain consisting of 610 amino acids. Albumin has two ends, the N-terminal end and the C-terminal end. The N-terminal amino acid residue is aspartic acid and the C-terminal residue is leucine. Serum albumin is composed of large amounts of essential amino acids such as arginine, histidine, and lysine, and the acidic amino acids aspartic acid and glutamic acid, as well as small amounts of tryptophan.

3 Different Types Of Proteins And Their Functions

Albumin is divided into two types depending on whether or not it contains a free sulfhydryl group (S-H). About two-thirds of blood serum albumin contains a free S-H group, and in the presence of Hg++ it tends to readily polymerize to form a dimer. That is why it is called mercaptalbumin. The remaining third, which does not possess a free SH group, is non-mercaptalbumin, which has lost its polymerizability.

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The osmotic pressure of blood is measured by the number of particles per unit volume. The smaller the particles, the higher the resulting osmotic activity. The molecular weight of albumin is relatively small and its serum concentration is higher than that of other protein components. To be more precise, 75% of the osmotic pressure of blood colloids depends on albumin, so it is sufficient that the osmotic pressure of blood is mainly determined by albumin.

As you recall, alpha and beta globulins are transport proteins produced by the liver, whereas gamma globulins are part of the immune system and are produced by immune cells.

Alpha proteins are globular or spherical proteins that are highly active in alkaline or other electrically charged solutions. Their molecular weight is usually around 93 kDa.

The α1 fraction is second only to the albumin fraction in its electrophoretic migration. It contains various components of serum proteins, including α1-antitrypsin, α1-acid glycoprotein, and α1-lipoprotein. The biological function of α1-antitrypsin is to inhibit the activity of trypsin and chymotrypsin. On the other hand, the function of α1-acid glycoprotein is still unknown, but it probably inhibits hemagglutination of inactivated influenza virus and inactivates progesterone.

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Also, the α2 fraction contains the main components of α2-macroglobulin, haptoglobin and ceruloplasmin. Haptoglobin selectively binds to hemoglobin, while ceruloplasmin promotes oxidation and incorporates copper. By binding to proteolytic enzymes such as trypsin and plasmin, α2-macroglobulin causes them to lose their main enzymatic activity.

Beta globulins are globular proteins in blood plasma that are relatively more mobile than gamma globulins but less mobile than alpha globulins on the electrophoresis medium.

The most important component included in the β-fraction of globulins is transferrin. Of the β-globulins, transferrin is the most abundant, accounting for approximately 50% of this globulin fraction.

3 Different Types Of Proteins And Their Functions

Transferrin binds to iron below physiological pH and forms an iron-transferrin complex. In fact, one-third of serum transferrin is bound to iron. Complement is part of the immune system and its role is to form membrane-attacking complexes to destroy pathogens, activate the inflammatory response, aid in phagocytosis, and neutralize toxins. Other essential components are hemopexin and propedin.

Classification Of Domains In Predicted Structures Of The Human Proteome

Gamma globulins, or immunoglobulins, are a functionally and structurally diverse group of proteins synthesized by plasma cells. First of all, they are biologically active, they have characteristic antibody activity.

Second, they have a very similar chemical structure. The immunoglobulin unit molecule consists of four polypeptide chains held together by interchain disulfide and non-covalent bonds, including a pair of heavy polypeptide chains (H chains) and one pair of light polypeptide chains (L chains). The heavy chains, which have a molecular weight of about 60,000, are divided into five major classes γ, δ, α, μ, and ε, depending on their antigenic specificity. The light chains, which have a molecular weight of about 23,000, are the same in all immunoglobulin classes and are further divided into two types; κ (kappa) chain or K-type and

(lambda) circuit or L-type. Chains have variable and fixed parts. The variable parts contribute to the binding affinity of the globulin of the antibody to its specific antigen, and their amino acid sequences differ from each other. The C-terminal segment, called the constant portion, has an essentially constant amino acid sequence for a given type of chain. Based on five different heavy chains, there are five classes of Ig-IgM, IgA, IgG, IgE and IgD.

Blood coagulation is the conversion of soluble fibrinogen molecules into a solid clot using the catalytic activities of various blood coagulation factors. Of the coagulation factors in plasma, fibrinogen is found in the highest amount, holding the honor of coagulation factor I. It electrophoretically migrates as the φ fraction between the β and γ fractions. Fibrinogen consists of 2,900 amino acids that are made up of three pairs of different polypeptide chains: γ, β, and α.

Proteins: Properties, Structure, Types, Functions

Many substances circulating in the bloodstream are bound to plasma proteins. These include antibiotics, vitamins, metal ions, lipids and metabolic products such as bile pigments. Plasma proteins contain hormones such as gonadal steroids, adrenocorticoids, and thyroid hormones.

Approximately 97% of serum female and male hormones are bound to plasma proteins, especially albumin. Conjugated forms of glucuronides and sulfates are also bound to albumin.

Adrenocorticoids bind primarily to transcortin and also to albumin, but less frequently. About 90-95% of serum adrenocorticoids are bound to plasma proteins.

3 Different Types Of Proteins And Their Functions

In addition, thyroid hormones bind to thyroxine-binding globulin, albumin, and prealbumin, and more than 99.9% of thyroxine exists in bound form.

Peripheral Membrane Proteins

Just as calcium loses its physiological activity when bound to plasma proteins, hormones are physiologically active in free form but become inactive when bound to plasma proteins. This is one way the endocrine system is controlled.

Plasma proteins can be separated and measured by many methods. The most commonly used methods are agar or gel electrophoresis and various types of immunoassays.

Electrophoresis is a widely used laboratory technique that separates biomolecules such as DNA, RNA, and proteins based on their size and electrical charge. The technique is based on the principle that molecules of different sizes and charges will migrate at different rates through a matrix such as a gel or a capillary tube when exposed to an electric field.

In electrophoresis, the sample containing the molecules to be separated is applied to a gel or capillary tube that acts as a sieve. An electric current is then applied to the gel or tube, causing the molecules to migrate through the matrix. Smaller molecules will move more easily through the pores of the gel or tube and travel faster than larger molecules.

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To determine the size of molecules in a sample, standards of known sizes are separated on the same gel or tube and then compared to the sample. This allows researchers to estimate the size of unknown molecules

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