从大鼠脑和肝癌组织中纯化醛缩酶C

Purification of aldolase C from rat brain and hepatoma.

作者信息

Hatzfeld A, Elion J, Mennecier F, Schapira F

出版信息

Eur J Biochem. 1977 Jul 1;77(1):37-43. doi: 10.1111/j.1432-1033.1977.tb11638.x.

DOI:10.1111/j.1432-1033.1977.tb11638.x

PMID:198211

Abstract

An isolation procedure for rat brain aldolase C has been developed which also permits the isolation of aldolase C from experimental hepatomas. Certain enzymatic properties (specific activity and Michaelis constant towards the two specific substrates: fructose 1,6-biphosphate and fructose 1-phosphate) and physico-chemical properties (molecular weight, N-terminal amino-acid) of the two enzymes have been studied and compared. Moreover, an amino-acid analysis has been carried out for rat brain aldolase C. Within experimental errors, the two enzymes appear to be identical.

摘要

已开发出一种从大鼠脑分离醛缩酶C的方法，该方法也可用于从实验性肝癌中分离醛缩酶C。对这两种酶的某些酶学性质（比活性以及对两种特定底物：1,6-二磷酸果糖和1-磷酸果糖的米氏常数）和物理化学性质（分子量、N端氨基酸）进行了研究和比较。此外，还对大鼠脑醛缩酶C进行了氨基酸分析。在实验误差范围内，这两种酶似乎是相同的。