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大鼠脑丙酮酸羧化酶的纯化及性质

Purification and properties of rat brain pyruvate carboxylase.

作者信息

Mahan D E, Mushahwar I K, Koeppe R E

出版信息

Biochem J. 1975 Jan;145(1):25-35. doi: 10.1042/bj1450025.

DOI:10.1042/bj1450025
PMID:1238083
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1165183/
Abstract

Rat brain pyruvate carboxylase was purified 2000-fold and some of its properties and kinetic parameters were investigated. The use of (NH4)2SO4 gradient solubilization on a Celite column and precipitation with polyethylene glycol permitted purification to an estimated 20% purity. Except for a few subtle kinetic differences this enzyme is indistinguishable from rat liver pyruvate carboxylase.

摘要

大鼠脑丙酮酸羧化酶被纯化了2000倍,并对其一些性质和动力学参数进行了研究。在硅藻土柱上使用硫酸铵梯度溶解法以及用聚乙二醇沉淀法,可将其纯化至估计纯度为20%。除了一些细微的动力学差异外,这种酶与大鼠肝脏丙酮酸羧化酶没有区别。

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引用本文的文献

1
Inhibitors of Pyruvate Carboxylase.丙酮酸羧化酶抑制剂
Open Enzym Inhib J. 2010;3:8-26. doi: 10.2174/1874940201003010008.

本文引用的文献

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Relationship of C14o2 fixation to carbohydrate metabolism in retina.视网膜中C14o2固定与碳水化合物代谢的关系。
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PYRUVATE CARBOXYLASE. IV. PARTIAL REACTIONS AND THE LOCUS OF ACTIVATION BY ACETYL COENZYME A.丙酮酸羧化酶。IV。部分反应及乙酰辅酶A的激活位点。
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THE STABILITY CONSTANTS OF METAL-ADENINE NUCLEOTIDE COMPLEXES.金属 - 腺嘌呤核苷酸络合物的稳定常数
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