肝脏微粒体葡萄糖-6-磷酸酶系统的组蛋白激活机制：一种测定葡萄糖-6-磷酸酶活性的新方法。
The mechanism of histone activation of the hepatic microsomal glucose-6-phosphatase system: a novel method to assay glucose-6-phosphatase activity.
作者信息
Blair J N, Burchell A
机构信息
Department of Medicine, Ninewells Hospital and Medical School, University of Dundee, U.K.
出版信息
Biochim Biophys Acta. 1988 Feb 17;964(2):161-7. doi: 10.1016/0304-4165(88)90162-6.
The mechanism of activation of hepatic microsomal glucose-6-phosphatase (EC 3.1.3.9) by histone 2A has been investigated in both intact and disrupted microsomes. Histone 2A increased the Vmax and decreased the Km of glucose-6-phosphatase in intact microsomes but had no effect on glucose-6-phosphatase activity in disrupted microsomes. Histone 2A was shown to activate glucose-6-phosphatase in intact microsomes by disrupting the membrane vesicles and thereby allowing the direct measurement of the activity of the latent glucose-6-phosphatase enzyme. The study demonstrated that disrupting microsomes with histone 2A is an excellent method for directly assaying glucose-6-phosphatase activity as it poses none of the problems encountered with all of the previously used methods.
已在完整和破碎的微粒体中研究了组蛋白2A激活肝微粒体葡萄糖-6-磷酸酶（EC 3.1.3.9）的机制。组蛋白2A增加了完整微粒体中葡萄糖-6-磷酸酶的Vmax并降低了其Km，但对破碎微粒体中的葡萄糖-6-磷酸酶活性没有影响。结果表明，组蛋白2A通过破坏膜泡从而直接测量潜在葡萄糖-6-磷酸酶的活性来激活完整微粒体中的葡萄糖-6-磷酸酶。该研究表明，用组蛋白2A破坏微粒体是直接测定葡萄糖-6-磷酸酶活性的一种极佳方法，因为它不存在所有先前使用方法所遇到的问题。
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