大鼠肾上腺匀浆线粒体中的3-羟基类固醇脱氢酶活性。
3 -Hydroxy steroid dehydrogenase activity in the mitochondria of rat adrenal homogenates.
作者信息
Basch R S, Finegold M J
出版信息
Biochem J. 1971 Dec;125(4):983-9. doi: 10.1042/bj1250983.
Abstract
The activity of 3beta-hydroxy steroid dehydrogenase (EC 1.1.1.51) in the mitochondrial fraction of rat adrenal homogenates was approx. 31% of the total activity recovered after differential centrifugation and washing of the particulate fractions. Some 45% of the total activity was found in the microsomal fraction. The activity was assayed by a radioisotopic method devised in this laboratory for the purpose of studying small quantities of tissue and cell fractions. Satisfactory separation of the two fractions was demonstrated by electron microscopy of the pellets and by comparative recoveries of RNA, steroid 21-hydroxylase and cytochrome c oxidase in the various compartments. Analyses of the kinetics of the enzyme activity in the two fractions revealed no significant differences in apparent K(m) for pregnenolone, dehydroepiandrosterone or NAD(+), but demonstrated a distinct difference in the K(m) for NADP(+). pH optima and susceptibility to cyanoketone inhibition were similar in both fractions.
摘要
大鼠肾上腺匀浆线粒体部分中3β-羟基类固醇脱氢酶（EC 1.1.1.51）的活性约为差速离心并洗涤颗粒部分后回收的总活性的31%。约45%的总活性存在于微粒体部分。该活性通过本实验室设计的一种放射性同位素方法进行测定，用于研究少量组织和细胞部分。通过对沉淀进行电子显微镜检查以及比较各部分中RNA、类固醇21-羟化酶和细胞色素c氧化酶的回收率，证实了这两个部分的良好分离。对这两个部分中酶活性动力学的分析表明，孕烯醇酮、脱氢表雄酮或NAD⁺的表观K(m)没有显著差异，但NADP⁺的K(m)存在明显差异。两个部分的最适pH值和对氰基酮抑制的敏感性相似。
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