蛔虫丙酮酸脱氢酶复合体的纯化及性质
Purification and properties of the Ascaris pyruvate dehydrogenase complex.
作者信息
Komuniecki R, Komuniecki P A, Saz H J
出版信息
Biochim Biophys Acta. 1979 Nov 9;571(1):1-11. doi: 10.1016/0005-2744(79)90219-5.
The pyruvate dehyhdrogenase complex (pyruvate:lipoate oxidoreductase (decarboxylating and acceptor-acetylating), EC 1.2.4.1) has been isolated from Ascaris muscle mitochondria and purified to near homogeneity by differential centrifugation, (NH4)2SO4 fractionation and calcium phosphate gel-cellulose chromatography. It is similar in shape, size and physical characteristics to pyruvate dehydrogenase complexes isolated from mammalian sources. It has an absolute dependence on CoA, NAD+ and pyruvate for activity and is competitively inhibited by acetyl-CoA and NADH. However, much higher NADH/NAD+ ratios are necessary to inhibit activity, suggesting regulation by the more reduced state of the pyridine nucleotide pool in Ascaris mitochondria.
丙酮酸脱氢酶复合体（丙酮酸：硫辛酸氧化还原酶（脱羧并乙酰基化受体），EC 1.2.4.1）已从蛔虫肌肉线粒体中分离出来，并通过差速离心、硫酸铵分级分离和磷酸钙凝胶-纤维素柱色谱法纯化至接近均一。它在形状、大小和物理特性上与从哺乳动物来源分离的丙酮酸脱氢酶复合体相似。其活性绝对依赖于辅酶A、烟酰胺腺嘌呤二核苷酸（NAD⁺）和丙酮酸，并受到乙酰辅酶A和还原型烟酰胺腺嘌呤二核苷酸（NADH）的竞争性抑制。然而，抑制活性需要更高的NADH/NAD⁺比值，这表明蛔虫线粒体中吡啶核苷酸库的更还原状态参与调节。
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