The isolation and characterization of serum albumin from the ostrich (Struthio camelus).
Ostrich serum albumin (OsSA) was purified by a combination of heat fractionation and polyethylene glycol precipitation. Equilibrium centrifugation revealed a relative molecular mass of 71,666 for the purified monomer, whereas the presence of a dimeric form was confirmed by means of PAGE and SDS-PAGE analysis. Compared to other species, relatively high levels of proline, glycine, isoleucine and histidine together with lowered amounts of half cystine, phenylalanine and arginine were observed in OsSA. A single N-terminal aspartic acid was identified. Isolated chicken adipocytes revealed a significantly lower in vitro lipolytic responsiveness towards added glucagon when OsSA replaced bovine serum albumin (BSA) in the medium (Km = 6.359 and 1.135 nM, Vm = 36.70 and 46.72 nmol/hr/micrograms adipocyte DNA for OsSA and BSA respectively).
D000273:Adipose Tissue / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001717:Birds / Q000097:blood*; D002417:Cattle; D002645:Chickens; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008066:Lipolysis / Q000187:drug effects; D008297:Male; D008970:Molecular Weight; D051381:Rats; D012709:Serum Albumin / Q000302:isolation & purification* / Q000494:pharmacology; D013045:Species Specificity
D000596:Amino Acids; D012709:Serum Albumin