来自大鼠肝细胞溶胶的阿司匹林水解酯酶。

Aspirin hydrolyzing esterases from rat liver cytosol.

作者信息

Kim D H, Yang Y S, Jakoby W B

机构信息

Laboratory of Biochemistry and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.

出版信息

Biochem Pharmacol. 1990 Aug 1;40(3):481-7. doi: 10.1016/0006-2952(90)90546-w.

DOI:10.1016/0006-2952(90)90546-w

PMID:2383281

Abstract

Unlike most esterases, which are predominantly bound to the microsomal fraction, the enzymes hydrolyzing acetylsalicylic acid are present in an equal amount in the cytosol. Two soluble isozymes were purified to homogeneity from rat liver and characterized as serine esterases with a Mr of 35,000. Both had the wide substrate spectrum characteristic of enzymes active in detoxication. Both had a very low Km for acetylsalicylate. Three other cytoplasmic enzymes active with aspirin were observed but these differed in their high Mr (about 220,000) and their lack of reactivity with antibody to one of the homogeneous isozymes.

摘要

与大多数主要与微粒体部分结合的酯酶不同，水解乙酰水杨酸的酶在细胞溶质中的含量相等。从大鼠肝脏中纯化出两种可溶性同工酶，并将其鉴定为分子量为35,000的丝氨酸酯酶，使其达到同质。两者都具有在解毒中起作用的酶所特有的广泛底物谱。两者对乙酰水杨酸的米氏常数都非常低。还观察到另外三种对阿司匹林有活性的细胞质酶，但它们的高分子量（约220,000）以及与其中一种同质同工酶抗体缺乏反应性有所不同。