豌豆中3-磷酸甘油酸脱氢酶的分离与特性研究
The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas.
作者信息
Slaughter J C, Davies D D
出版信息
Biochem J. 1968 Oct;109(5):743-8. doi: 10.1042/bj1090743.
Abstract
- 3-Phosphoglycerate dehydrogenase was purified 400-fold from crude extracts of etiolated pea epicotyls. 2. Michaelis constants were determined for all four substrates. 3. Loss of sensitivity to inhibition by l-serine occurs on purification. 4. The purified enzyme is inhibited by thiol-group reagents and, with N-ethyl-maleimide, protection is afforded by 3-phosphoglycerate though not by NAD(+).
摘要
从黄化豌豆上胚轴的粗提物中纯化出了3-磷酸甘油酸脱氢酶，纯化倍数为400倍。
测定了所有四种底物的米氏常数。
纯化过程中对L-丝氨酸抑制的敏感性丧失。
纯化后的酶受到巯基试剂的抑制，对于N-乙基马来酰亚胺，3-磷酸甘油酸可提供保护作用，但NAD(+)不能。
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