大鼠肝脏可溶性磷脂酸磷酸水解酶的部分纯化及特性分析
Partial purification and characterization of the soluble phosphatidate phosphohydrolase of rat liver.
作者信息
Butterwith S C, Hopewell R, Brindley D N
出版信息
Biochem J. 1984 Jun 15;220(3):825-33. doi: 10.1042/bj2200825.
Abstract
A method is described by which the Mg2+-stimulated phosphatidate phosphohydrolase can be purified from the soluble fraction of liver from ethanol-treated rats. The increase in specific activity was about 416-fold. This involved purification by adsorption on calcium phosphate, chromatography on DE-52 DEAE-cellulose, separation on Ultrogel AcA-34 and chromatography on CM-Sepharose 6B. The effects of phosphatidylcholine, phosphatidate and Mg2+, Mn2+ and Zn2+ on the activity are described. Inhibitor studies indicate that the phosphohydrolase contains functional thiol groups and arginine residues.
摘要
本文描述了一种从乙醇处理大鼠肝脏的可溶性部分中纯化镁离子刺激的磷脂酸磷酸水解酶的方法。比活性增加了约416倍。这包括通过磷酸钙吸附纯化、DE-52 DEAE-纤维素柱色谱、Ultrogel AcA-34分离以及CM-Sepharose 6B柱色谱。描述了磷脂酰胆碱、磷脂酸以及镁离子、锰离子和锌离子对该酶活性的影响。抑制剂研究表明，该磷酸水解酶含有功能性巯基和精氨酸残基。
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