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[人培养细胞中葡萄糖-6-磷酸脱氢酶的分离及性质]

[Isolation and properties of glucose-6-phosphate dehydrogenase from human cultivated cells].

作者信息

Alekseev S B, Mamaev V B, Stepanova L G, Kalinina L I, Avakova A N

出版信息

Biokhimiia. 1979 May;44(5):940-6.

PMID:454722
Abstract

A new procedure for purification of glucose-6-phosphate dehydrogenase resulting in an electrophoretically homogenous preparation made up of 5.10(8) cells (390 mg of protein) is proposed. The enzyme yield is more than 20%. The molecular weights of a subunit and a native enzyme are 55000 and 220000, respectively. The isoelectric point for the protein lies at 4,8. The kinetics of the enzyme thermal inactivation obey the first order equation with the inactivation rate constant of 6.10(-3) min-1.

摘要

提出了一种纯化葡萄糖-6-磷酸脱氢酶的新方法,该方法可得到由5×10⁸个细胞(390毫克蛋白质)组成的电泳纯制剂。酶的产率超过20%。亚基和天然酶的分子量分别为55000和220000。该蛋白质的等电点为4.8。酶热失活动力学符合一级方程,失活速率常数为6×10⁻³分钟⁻¹。

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