Purification and characterization of the sex steroid binding protein from macaque serum. Comparison with the human protein.
Purification and characterization of the sex steroid binding protein from macaque serum. Comparison with the human protein.
复制标题
猕猴血清中性类固醇结合蛋白的纯化和表征。
DOI：
10.1021/bi00298a014
复制
发表时间：
1984
期刊：
影响因子：
2.9
通讯作者：
Petra,PH
中科院分区：
文献类型：
--
作者：
Turner,EE;Ross,JB;Namkung,PC;Petra,PH
摘要：猕猴性类固醇结合蛋白(SBP)已被纯化为均一性类固醇结合蛋白(SBP)，并对其进行了化学鉴定。天然蛋白是一种糖蛋白，经十二烷基硫酸钠凝胶电泳法测定，其分子量约为88000，由两个相似的亚基组成，分子量47000。在11℃时，一个5a-二氢睾酮分子与每个二聚体结合，其Kd值等于1.6 nM。
Eric E. Turner, J. B. Alexander Ross, Pearl C. Namkung, and Philip H. Petra* abstract: The sex steroid binding protein (SBP) of Macaca mulatto and Macaca nemestrina sera has been purified to homogeneity and chemically characterized. The native protein is a glycoprotein having a molecular weight of approximately 88 000 and is composed of two similar subunits of molecular weight 47 000 as estimated by sodium dodecyl sulfate gel electrophoresis. One molecule of 5a-dihydrotestosterone is bound per dimer with a KD equal to 1.6 nM at 11 C.