YEAST DIPHOSPHOPYRIDINE NUCLEOTIDE SPECIFIC ISOCITRATE DEHYDROGENASE - PURIFICATION AND SOME PROPERTIES
YEAST DIPHOSPHOPYRIDINE NUCLEOTIDE SPECIFIC ISOCITRATE DEHYDROGENASE - PURIFICATION AND SOME PROPERTIES
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DOI：
10.1021/bi00797a022
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发表时间：
1971-01-01
期刊：
影响因子：
2.9
通讯作者：
ATKINSON, DE
中科院分区：
文献类型：
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作者：
BARNES, LD;KUEHN, GD;ATKINSON, DE
Larry D.巴恩斯，f Glenn D. Kuehn，t和丹尼尔E. Atkinson §摘要：酵母二磷酸吡啶核苷酸特异性异柠檬酸脱氢酶（EC 1.1。1.41）已通过盘状凝胶电泳、沉降速度和沉降平衡标准纯化为同源重组。通过用柠檬酸盐（酶的改性剂）优先从离子交换柱洗脱酶来促进酶的纯化。柠檬酸盐还在分离过程中稳定酶，并保持与异柠檬酸盐的动力学协同性。通过沉降平衡测定，该酶的表观分子量为3 × 105。A亚基分子
Larry D. Barnes, f Glenn D. Kuehn, t and Daniel E. Atkinson § abstract: Yeast diphosphopyridine nucleotide specific isocitrate dehydrogenase (EC 1.1. 1.41) has been purified to homo-geneity by the criteria of disc gel electrophoresis, sedimentation velocity, and sedimentation equilibrium. Purification of the enzyme is facilitated by preferentially eluting the enzyme from ion-exchange columns with citrate, a modifier of the enzyme. Citrate also stabilizes the enzyme during isolation and pre-serves the kinetic cooperativity with respect to isocitrate. The enzyme has an apparent molecular weight of 3 X 105 as determined by sedimentation equilibrium. A subunit molecular