Hanquez-Laurent C, de Lauzon S, Cittanova N
J Steroid Biochem. 1982 Dec;17(6):647-51. doi: 10.1016/0022-4731(82)90566-0.
The conditions for the solubilization of 17 beta-hydroxysteroid dehydrogenase from a rat liver microsomal preparation with the non-ionic detergent Triton X-100 were studied. The recoveries of 17 beta-hydroxysteroid dehydrogenase activity and of proteins in the solubilized form were determined as a function of detergent concentration, of pH and temperature, of incubation time and of saline concentration. The soluble fraction obtained under the optimal conditions contained 80% of the proteins and 75% of the enzymatic activity of initial microsomes. The presence of Triton X-100 in the solubilized proteins was not essential for enzyme activity.
研究了用非离子去污剂Triton X-100从大鼠肝脏微粒体制剂中增溶17β-羟基类固醇脱氢酶的条件。测定了增溶形式的17β-羟基类固醇脱氢酶活性和蛋白质回收率与去污剂浓度、pH值和温度、孵育时间以及盐浓度的关系。在最佳条件下获得的可溶部分含有初始微粒体80%的蛋白质和75%的酶活性。增溶蛋白中Triton X-100的存在对酶活性并非必需。
