鸵鸟（鸵鸟属骆驼鸵鸟）血清白蛋白的分离与鉴定。

The isolation and characterization of serum albumin from the ostrich (Struthio camelus).

作者信息

Bradley G, Naudé R J, Oelofsen W

出版信息

Comp Biochem Physiol B. 1985;82(4):829-35. doi: 10.1016/0305-0491(85)90531-0.

Abstract

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).

摘要

通过热分级分离和聚乙二醇沉淀相结合的方法纯化了鸵鸟血清白蛋白（OsSA）。平衡离心显示纯化单体的相对分子质量为71,666，而通过PAGE和SDS-PAGE分析证实存在二聚体形式。与其他物种相比，在OsSA中观察到脯氨酸、甘氨酸、异亮氨酸和组氨酸水平相对较高，同时半胱氨酸、苯丙氨酸和精氨酸的含量较低。鉴定出一个单一的N端天冬氨酸。当OsSA替代培养基中的牛血清白蛋白（BSA）时，分离的鸡脂肪细胞对添加的胰高血糖素的体外脂解反应性显著降低（OsSA和BSA的Km分别为6.359和1.135 nM，Vm分别为36.70和46.72 nmol/hr/μg脂肪细胞DNA）。