find out the percentage and functions of different blood proteins
Answers
Answer:
Total Protein, Albumin, Total Globulin, and Albumin/Globulin Ratio
Total serum protein concentration reflects all of the different proteins in plasma with the exception of those that are consumed in clot formation, such as fibrinogen and the clotting factors. Over 1000 individual proteins have been characterized in serum. Most are not biochemically pure proteins, but are proteins combined with other substances. Plasma protein is about 0.3–0.5 g/L greater than serum protein. Albumin accounts for about 50% of total serum protein concentration in most species, and for about 75% of plasma colloidal activity. Albumin synthesis occurs in the liver. There is a direct correlation between body size and albumin turnover (e.g., plasma albumin half-life is 2 days in mice and 8 days in dogs).
Globulins constitute a number of heterogeneous proteins, including coagulation factors, transport proteins, and mediators of inflammation and immunoglobulins. Most globulins are synthesized by hepatocytes; the major exceptions are the immunoglobulins that are produced by B lymphocytes and plasma cells. Electrophoretic separation identifies alpha, beta, and gamma fractions, although protein electrophoresis is not generally included in most non-clinical toxicology protocols. Albumin/globulin (A/G) ratios reflect changes in the two major protein types. The hydration status of the animal should be considered when interpreting protein changes. Low serum protein, like anemia, can be masked by dehydration. Albumin and globulins are increased proportionately in simple dehydration.
Medical Biotechnology and Healthcare
X. Lu, ... Z. Su, in Comprehensive Biotechnology (Second Edition), 2011
5.54.3.2.4 Protein conjugated Hb
Blood proteins such as serum albumin, superoxide dismutase (SOD), and catalase (CAT) have been conjugated to Hb to form macromolecules, which provide not only larger MW to prolong the circulation but also, the function of other key proteins in the blood. The Chang group developed a new generation of polyHb based on cross-linking polyHb with SOD and CAT (PolyHb–SOD–CAT), which can transport oxygen and at the same time remove oxygen radicals so as to lessen the effects of ischemia–reperfusion injuries [10]. The conjugation of two major blood proteins, Hb and human serum albumin, combines the function of oxygen carrier and volume expander, and facilitates the modified Hb closer to a real blood substitute [30].
The manufacturing process of cross-linked Hb and poly-Hb is relatively simple, but the products are not uniform. The concern of inducing an immune response is always present with these products. A solid-phase adsorption method was proposed to prepare well-defined bovine serum albumin (BSA)–bovine Hb conjugate. After adsorption by the solid phase, BSA molecules were allowed to react with GDA. The spacing out of BSA molecules on the solid phase was assumed to limit polymerization of BSA molecules, except some molecules bound closely on the solid phase, resulting in a minor dimer formation [16]. Conjugated Hb can be obtained as homogeneous products and concern related to antigenicity can be eliminated. They have longer circulation half-lives which are similar to the regeneration of erythrocytes in the body.
It was recently reported that cell-free Hb increased the risk of myocardial infarction and death in a meta-analysis over five distinct products: HemAssist (Baxter Healthcare Corp., Deerfield, IL, USA), Hemopure (Biopure Corp., Cambridge, MA, USA), Hemolink (Hemosol BioPharma Inc., Ontario, Canada), Poly-Heme (Northfield Laboratories Inc., Evanston, IL, USA), and Hemospan (Sangart Inc., San Diego, CA, USA) [30]. Major disadvantages of cell-free Hb are thought to derive from systemic vasoconstriction and decreased tissue blood flow as a result of scavenging nitric oxide, in spite of chemical modifications of Hb such as cross-linking and polymerization.
Answer:
Globulins make up 38% of blood proteins and transport ions, hormones, and lipids assisting in immune function. Fibrinogen comprises 7% of blood proteins; conversion of fibrinogen to insoluble fibrin is essential for blood clotting.