[细菌膜蛋白。溶壁微球菌NADH脱氢酶的性质]
[Bacterial membrane proteins. Properties of Micrococcus lysodeikticus NADH dehydrogenase].
作者信息
Zhukova I G, Kharat'ian E F, Ostrovskiĭ D N
出版信息
Biokhimiia. 1979 May;44(5):811-5.
PMID:454711
Abstract
NADH dehydrogenase was isolated from M. lysodeikticus membranes with FAD as a prosthetic group. It was found the enzyme molecular weight is about 140000 in 0,01 M phosphate buffer, pH 7,4 in 1% Triton X-100. The enzyme molecules are dimers consisting of two subunits with molecular weight of 70000. The content of alpha-helical regions is 30%, that of beta-forms is 13%. The protein globule is cross-linked with the disulfide bonds and has hydrophobic regions on its surface.
摘要
从溶壁微球菌膜中分离出以黄素腺嘌呤二核苷酸（FAD）作为辅基的NADH脱氢酶。发现在含1% Triton X - 100、pH 7.4的0.01 M磷酸盐缓冲液中，该酶的分子量约为140000。酶分子是由两个分子量为70000的亚基组成的二聚体。α - 螺旋区域的含量为30%，β - 折叠形式的含量为13%。蛋白质球通过二硫键交联，其表面有疏水区域。
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