小鼠磷酸甘油酸变位酶同工酶的纯化及性质

Purification and properties of the phosphoglycerate mutase isozymes from the mouse.

作者信息

Fundele R, Krietsch W K

出版信息

Comp Biochem Physiol B. 1985;81(4):965-8. doi: 10.1016/0305-0491(85)90098-7.

DOI:10.1016/0305-0491(85)90098-7

Abstract

The two homodimeric isozymes of phosphoglycerate mutase have been purified from murine kidney and muscle. No differences were observed in the Michaelis-Menten constant for the substrate 2-phospho-D-glycerate, in molecular weight, temperature and pH optima, when the purified isozymes were compared. The isozymes differ in their inhibition constants for phosphoenolpyruvate, in their Michaelis constants for 3-phospho-D-glycerate and 2,3-bisphospho-D-glycerate, their thermal and pH lability and in their sensitivity towards mercury ions.

摘要

磷酸甘油酸变位酶的两种同二聚体同工酶已从鼠肾和肌肉中纯化出来。当对纯化的同工酶进行比较时，发现它们在底物2-磷酸-D-甘油酸的米氏常数、分子量、温度和pH最佳值方面没有差异。这些同工酶在对磷酸烯醇丙酮酸的抑制常数、对3-磷酸-D-甘油酸和2,3-二磷酸-D-甘油酸的米氏常数、它们的热稳定性和pH稳定性以及对汞离子的敏感性方面存在差异。

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