Albumin Reversion of Thrombocytopenia Using Bovi

B. Albumin

B.1 Description Albumin is a small, multifunctional, non-glycoselated, negatively charged plasma protein. It contributes over 50 of the total plasma protein. It is an umbrella term for a type of protein which is water soluble. Numerous types of albumin can be found all over the natural world, and two of the most familiar examples of albumin can be found in egg whites and in human blood. Albumin is an important class of protein, and they are vitally important to health and well being for many organisms. Many plants and animals contain or secrete albumin Wisegeek [updated 2010]. Albumins are usually named according to where they are found in nature. For example, the albumin found in human blood serum is called human serum albumin HSA. Albumins contain, in all cases, the elements carbon, hydrogen, nitrogen, sulphur and oxygen; their composition, however, varies within certain limits. They also contain small amounts of carbohydrates and phosphoric acid. Its chemical formula is C 720 H 1134 N 218 S 50241 Encyclopedia.org [updated 2006]. Albumin has high molecular weights. The various forms of albumins have a molecular weight ranging from about 34,000-70,000 gmol. It is produced exclusively in the liver and secreted directly into the circulation. The half-life of albumin in the circulation is about 20 days and the liver has large reserves of albumin synthetic capacity Sydpatd [updated 2001]. Human serum albumin HSA is the most abundant plasma protein found in humans, accounting for 55-60 of the measured serum protein. It consists of a single polypeptide chain of 585 amino acids with a molecular weight of 66,500 gmol Articleonlinedirectory [updated 2010]. Bovine serum albumin BSA is a large globular protein with a molecular weight of 66,000 gmol in cows. BSA binds free fatty acids, other lipids, and flavor compounds, which can alter the heat denaturation of the protein. Its primary biological function has been associated with its lipid binding properties. BSA is cheap and plentiful due to the fact thats its a natural byproduct of the cattle industry. This makes it ideal in vaccine production, medical research, and food additives. BSA is essentially a plasma protein that can be used to grow cells, test the proteins of other cells, and be added to a variety of food products. BSA is quite stable, which makes it ideal for scientific measures Articleonlinedirectory [updated 2010]. BSA is a common agent used in restriction digest to stabilize enzymes during the digestion of DNA for study. Albumin does not affect other enzymes that don‘t use it to maintain stabilization. This makes bovine serum albumin essential for determining the amount of proteins present with great accuracy. Research shows that BSA is highly effective at reducing the probability of disease. Its advantages in treating disease make BSA a common ingredient in vaccines and other medicines. BSA is also widely used in cell regeneration. You can readily use albumin to regenerate plants from cultured guard cells. BSA greatly enhances cell production with a healthy dose of protein. BSA is also a common supplement in dietary products because it is so inexpensive. Albumin can be turned into whey that is then cooked into your pastry, chocolate brownie or dipping sauce republicanforaday [updated 2010]. B.2 Production of Albumin Albumin is synthesized in the liver at a rate of 9-12 g per day in normal adults. Under physiological circumstances only 20 –30 of hepatocytes produce albumin and synthesis can therefore be increased on demand by a factor of 200 –300. Changes in the rate of production are governed primarily by alterations in colloid osmotic pressure, and the osmolality of the extravascular hepatic space. Albumin levels are dependent on the rate of synthesis: 1 the amount secreted from the liver cell, 2 the distribution in body fluids, and 3 the level of degradation. Albumin is distributed into the extravascular spaces of all tissues, with the majority being distributed in the skin. Approximately 30-40 of albumin in the body is found within the vascular compartments of the muscle, skin, liver, gut, and other tissues. Albumin enters the intravascular space via two pathways. First, albumin enters this space by entering the hepatic lymphatic system and moving into the thoracic duct. Second, albumin passes directly from hepatocytes into the sinusoids after traversing the Space of Disse, the space separating sinusoids from hepatocytes. Albumin has a circulation half-life of 16-18 hours. Albumin distributes into the hepatic interstitial volume, and the concentration of colloids in this small volume is an osmotic regulator for albumin synthesis. This is the principal regulator of albumin synthesis during normal periods without stress. Degradation of albumin is poorly understood. After secretion into the plasma, the albumin molecule passes into tissue spaces and returns to the plasma via the thoracic duct. Studies suggest that albumin may be degraded within the endothelium of the capillaries, bone marrow, and liver sinuses. Albumin molecules apparently degrade randomly, with no differentiation between old and new molecules. Albumin degradation occurs at a rate of 9-12 g or 4 of total body albumin per day. Factors that accelerate albumin degradation are protein and calorie malnutrition, stress, trauma and septicemia. Any derangement in one or more of these processes will result to hypoalbuminemia, or abnormally low levels of albumin. B.3 Role of Albumin in the Human Body A review done by Abhasnee Sobhonslidsuk 2009 on human serum albumin enumerated the 5 major roles of albumin in the human body. It contributes to the 1 colloid osmotic pressure effect, 2 binding and transport of molecules, 3 free radical scavenging, 4 platelet function inhibition and anti-thrombotic effects, and 5 capillary membrane permeability. For the colloid osmotic pressure effect, since albumin contributes to 60 of the intravascular protein, it provides 60 of the colloid osmotic pressure. Albumin attracts sodium ions by means of the negatively charged property, resulting in water retention and colloid osmotic pressure effect. For the binding and transport of molecules, albumin can bind weakly and reversibly to drugs and metabolites including bilirubin, fatty acid, thyroxin, etc. because of its strong negative charge. For the free radical scavenging, the abundant sulphydryl groups found in albumin scavenge for reactive oxygen and nitrogen species. For the platelet function inhibition and anti-thrombotic effects, the albumin inhibits the rapid inactivation of nitric oxide and allows prolongation of its anti- aggregatory effects on platelets. Lastly, for the capillary membrane permeability, albumin may directly influence vascular integrity by binding in the interstitial matrix and subendothelium and by altering permeability of these layers to large molecules and solutes. B.4 Other Forms of Albumin and Their Sources Numerous types of albumin can be found all over the natural world, and two of the most familiar examples of albumin can be found in egg whites and in human blood. Albumin is an important class of protein, and they are vitally important to health and well being for many organisms. Many plants and animals contain or secrete albumin Wisegeek [updated 2010]. Albumins are usually named according to where they are found in nature. For example, the albumin found in human blood serum is called human serum albumin HSA. Protein and Source Abbreviation Reference Albumin Human HSA Behrens et al. 1975 Meloun et al. 1975 Lawn et al 1981 Dugaiczyk et al. 1982 Bovine BSA Brown 1975 Holowachuk 1991 Equine ESA Ho et al. 1993 Rat RSA Sargent et al. 1981 Mouse MSA Minghetti et al. 1985 Pig PSA Weinstock and Baldwin 1988 Sheep OSA Brown et al. 1989 Frog XSA Haefliger et al. 1989 Salmon SSA Byrnes and Gannon 1990 Lamprey LSA Gray and Doolittle 1992 α-Fetoprotein Human AFP Law and Dugaiczyk 1981 Rat ---- Jagodzinski et al. 1981 Mouse ---- Gorin et al. 1981 Vtamin D-binding protein Human VDP Yang et al. 1981 Schoentgen et al. 1986 Rat ---- Cooke and David 1985 Mouse ---- Yang et al. 1990 Figure 1. Other forms of albumin and their sources

C. Relationship Between Platelets and Albumin