Normal human serum albumin

Albuconn albumin human solution Albuminar Albumisol Albuspan Albutein Buminate human serum albumin normal human serum albumin Plasbumin plasma albumin Pro-Butnin Proserum. 

Gellis, S. S. Neefe, J. R. Stokes, J. Stong, L. E. Janeway, C. A. and Scatchard, G. "Chemical, clinical, and immunological studies on the virus of homologous serum hepatitis in solutions of normal human serum albumin by means of heat" J. Clin. Invest. 1948. 27 239-244. 

S1I -labelled form, iodinaled (,lll) human serum albumin, J,f HSA, Albumotope u,f, Macroscan-131, Risa-I31-H. Normal human serum albumin mildly jodinated with radio-active iodine (1311) which has a half-life of 8 days, and emits beta and gamma rays. Contains not more than one atom of iodine par molecule of albumin (mol wt 60,000). Physical and chemical proparties essentially the same as those of albumin. Stable at 10° for at least 3 weeks. Supplied for injection in aq isotonic sodium chloride soln. 

Human serum albumin 582 amino acids 17 disulphide bridges Yeast Plasma replacement therapy Normally obtained from plasma but now concern over potential contamination with AIDS virus... 

Most frequently, binding protein is added to the incubation mixtures as either serum or purified serum albumin. With human serum albumin, at equilibrium, the acceptor substrate will largely be protein-bound, when the bilirubin albumin molecular ratio is smaller than one (the dissociation constant of the first binding site of purified human serum albumin is approximately 7 X 10 M with 2 X 10 M for two additional binding sites) (J2). The first binding site of albumin, measured with rat serum, has a dissociation constant of about 5 X 10" M (M8). The unbound fraction will normally not exceed the very low solubility of the pigment. Addition of albumin to an alkaline solution of bilirubin, or its addition immediately after neutralization, prevents colloid formation, if the bilirubin albumin molecular ratio is smaller than one (B25). However, colloidal bilirubin, once formed, cannot be redissolved by the addition of albumin (B26). 

Human serum albumin (HSA) is the single most abundant protein in blood (Table 9.4). Its normal concentration is approximately 42g/litre, representing 60% of total plasma protein. The vascular system of an average adult thus eontains in the region of 150 g of albumin. HSA is responsible for over 80% of the colloidal osmotic pressure of human blood. More than any other plasma constituent, HSA is thus responsible for retaining sufficient fluid within blood vessels. It has been aptly described as the protein that makes blood thicker than water. 

Protein disulfide isomerase and Erolp are enzymes that help form disulfide bonds within the endoplasmic reticulum. These factors are critical for the normal formation of disulfide bonds during protein folding. See Lodi, T., Neglia, B., and Donnini, C., Secretion of human serum albumin by... 

Fig. 24. Immunoelectrophoresis of human gastric juice. Immunoelectrophoietic patterns A, in vitro depepsinized normal gastric juice B, crystalline human pepsin C, crystalline human gastricsin D, human serum albumin E, glandular mucoprotein F, mucoproteose C, rapid vitamin Bj2 binder H, slow vitamin B 2 binder. Anti-gastric juice immune serum was used throughout. From Simons and Grasbedc (S9).

Mutations in a human serum albumin gene that substitute either histidine or proline for arginine at position 218 increase binding affinity for T4. These mutations are autosomal dominant and occur with relatively high frequency. Carriers of these mutations have high levels of total serum T4 but their free-T4 and TSH concentrations are within the normal range. Individuals are euthyroid (normal thyroid) and their conditions are known as familial dysalbumine-mic hyperthyroxinemia (FDH). 

Analbuminemia is a rare autosomal recessive disorder. Affected individuals do not exhibit serious clinical symptoms, not even edema. The lack of clinical edema is presumably due to osmotic compensation by the mildly elevated globulins. Osteoporosis in analbuminemia has been corrected by the administeration of human serum albumin. Affected females exhibit minimal pretibial edema, mild anemia, normal liver function tests, absence of proteinuria, lowered blood pressure, elevated serum cholesterol levels, and lipodystrophy. Despite elevated plasma cholesterol levels, severe atherosclerosis was not present. 

Peripheral blood mononuclear cells were obtained by density gradient separation through Ficol-Hypaque technology 17). Thymidine incorporation proliferation assays were set up as previously described using human serum albumin (HSA) or STn-HSA as stimulant (77). A stimulation index of > 2 SD compared to normal donors mononuclear cells was used as evidence of positive response. Fifty seven percent of tested vaccinated patients had evidence of specific T cell proliferation against STn. 

The specificity of the ELISA method for Mn-SOD was examined. None of the major proteins found in human sera or erythrocytes (such as human serum albumin human a-, (3-, or y-globulin Cu,Zn-SOD or hemoglobin) showed a reaction with this method. To test the possibility of assaying the enzyme in human sera, three different concentrations of Mn-SOD were added to normal human serum and the effect of dilution on the ELISA was examined. A linear relationship was observed between the immunoreactive Mn-SOD level and the serum dilution in the range of 8- to 128-fold (Fig. 13). The ELISA was performed as described in Section 3,4,2,1, wherein a serum sample is diluted 10- or 11-fold and used for the assay. 

Figure 7.9 Right X-ray structure of the Human serum albumin (HSA) protein and molecular structure ofthe used ligand HPMO. Left Schematic representation of a normal micelle structure (left top) X-ray structure of/ -cyclodextrin (left middle), and illustration of a protein-ligand recognition process (left bottom) [58].

Personal experience has proved the excellent quality of the horse immune serum against normal human serum from Serpasteur (36 rue du Dr. Roux, Paris 15 ). For injection, 200 ml of a Red Cross plasma pool is mixed with 200 ml of Bayol-F and 70 ml of Arlacel (W5) 9 subcutaneous injections of doses of 2.5 ml are given over a 40-day period. After an 80-day interval, a second series of 7 injections is administered. Serum from the withdrawn blood is sterilized by filtration and sealed in ampoules with Merthiolate at 1 10,000. The same laboratory has produced a horse antiserum against human serum albumin (W5) by a series of 39 intramuscular injections of a 5 % solution of Fraction V over a period of 4J4 months. 

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