牛肝中四氢叶酸-蛋白质复合物的纯化与特性分析

Purification and characterization of tetrahydrofolate.protein complex in bovine liver.

作者信息

Watabe S

出版信息

J Biol Chem. 1978 Oct 10;253(19):6673-9.

Abstract

Gel filtration of bovine liver extract on a Sephadex G-200 column resolved three macromolecular fractions with dihydropteridine reductase-dependent cytochrome c reducing activity. One of the active fractions was purified from the extract through the steps of solvent fractionation, chromatography on DEAE-Sephadex, and gel filtration. Biochemical and microbiological analyses showed that the purified complex consists of a Mr = 70,000 protein and tetrahydropteroyldiglutamate. In contrast to the extreme lability of free tetrahydropteridines the complex was quite stable against autooxidation under aerobic conditions.

摘要

牛肝提取物在葡聚糖凝胶G - 200柱上进行凝胶过滤，分离出三个具有依赖二氢蝶啶还原酶的细胞色素c还原活性的大分子级分。其中一个活性级分通过溶剂分级分离、DEAE - 葡聚糖凝胶柱色谱和凝胶过滤等步骤从提取物中纯化得到。生化和微生物分析表明，纯化后的复合物由一种分子量为70,000的蛋白质和四氢蝶酰二谷氨酸组成。与游离四氢蝶啶的极端不稳定性相反，该复合物在有氧条件下对自动氧化相当稳定。