磷酸甘油酰基转移酶同工酶存在的证据。
Evidence for the existence of isoenzymes of glycerol phosphate acyltransferase.
作者信息
Nimmo H G
出版信息
Biochem J. 1979 Jan 1;177(1):283-8. doi: 10.1042/bj1770283.
Abstract
Subcellular-fractionation studies confirmed previous findings that rat liver glycerol phosphate acyltransferase was located in both mitochondria and the microsomal fraction. Studies of the two activities revealed several differences between them. The mitochondrial enzyme had a lower Km for sn-glycerol 3-phosphate and was more resistant to heat inactivation than was the microsomal enzyme. Some preparations of the mitochondrial enzyme were inhibited by high concentrations of glycerol phosphate. The mitochondrial enzyme was not inactivated by thiol-group reagents, whereas the microsomal enzyme was very rapidly inactivated by these compounds. However, the microsomal enzyme could be specifically protected against this inactivation by low concentrations of palmitoyl-CoA. The results indicate the existence of distinct isoenzymes of glycerol phosphate acyltransferase with different intracellular locations.
摘要
亚细胞分级分离研究证实了先前的发现，即大鼠肝脏甘油磷酸酰基转移酶存在于线粒体和微粒体部分。对这两种活性的研究揭示了它们之间的几个差异。线粒体酶对sn-甘油3-磷酸的Km值较低，并且比微粒体酶更耐热失活。线粒体酶的一些制剂会受到高浓度甘油磷酸的抑制。线粒体酶不会被巯基试剂灭活，而微粒体酶会被这些化合物非常迅速地灭活。然而，低浓度的棕榈酰辅酶A可以特异性地保护微粒体酶免受这种灭活。结果表明存在具有不同细胞内定位的甘油磷酸酰基转移酶的不同同工酶。
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