Poliakova E D, Dizhe E B, Klimova T A, Petrova L A, Klimov A N
Biokhimiia. 1976 Nov;41(11):2037-42.
Assay conditions are worked out for determination of activity of beta-hydroxy-beta-methylglutaryl-CoA reductase (HMG-CoA reductase) in 140.000 g supernatant fraction of the rat liver. Some kinetic properties of the enzyme are studied: the activity dependency on the incubation time, protein concentration, pH, glutathione, dithiothreitol and HMG-CoA contents in the incubation medium. The effect of Triton WR 1339 on the activity of HMG-CoA reductase in the liver 140.000 g supernatant and microsomal fractions is comparatively studied. Diurnal activity variations of soluble and microsomal enzymes are also investigated. It is suggested that the rat liver HMG-CoA reductase in the 140.000 g supernatant fraction is not identical to the enzyme located in the microsomal fraction.
确定大鼠肝脏140,000g上清液组分中β-羟基-β-甲基戊二酰辅酶A还原酶（HMG-CoA还原酶）活性的测定条件已确定。研究了该酶的一些动力学特性：活性对孵育时间、蛋白质浓度、pH、谷胱甘肽、二硫苏糖醇和孵育介质中HMG-CoA含量的依赖性。比较研究了Triton WR 1339对肝脏140,000g上清液和微粒体组分中HMG-CoA还原酶活性的影响。还研究了可溶性和微粒体酶的昼夜活性变化。提示大鼠肝脏140,000g上清液组分中的HMG-CoA还原酶与微粒体组分中的酶不同。
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