牛心线粒体中依赖NADP的异柠檬酸脱氢酶的纯化及性质
The purification and properties of NADP-dependent isocitrate dehydrogenase from ox-heart mitochondria.
作者信息
Macfarlane N, Mathews B, Dalziel K
出版信息
Eur J Biochem. 1977 Apr 15;74(3):553-9. doi: 10.1111/j.1432-1033.1977.tb11424.x.
Abstract
The purification of NADP-linked isocitrate dehydrogenase from ox heart mitochondria is described. The molecular weight from gel filtration, sedimentation equilibrium and gel electrophoresis is 90000+/-4000, and there are two subunits in the molecule each of which binds NADPH with enhancement of the coenzyme fluorescence. The amino-acid composition is reported, and the absorption coefficient, A1/280%, estimated from dry weight measurements is 11.8 cm-1.
摘要
本文描述了从牛心线粒体中纯化NADP连接的异柠檬酸脱氢酶的方法。通过凝胶过滤、沉降平衡和凝胶电泳测得其分子量为90000±4000，该分子中有两个亚基，每个亚基结合NADPH时会增强辅酶荧光。文中报道了其氨基酸组成，根据干重测量估算的吸收系数A1/280%为11.8 cm-1。
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