日本鳗鲡阴离子胰蛋白酶的特性分析。

Characterization of an anionic trypsin from the eel (Anguilla japonica).

作者信息

Yoshinaka R, Sato M, Suzuki T, Ikeda S

出版信息

Comp Biochem Physiol B. 1985;80(1):11-4. doi: 10.1016/0305-0491(85)90415-8.

Abstract

An enzyme, isolated from the pancreas of the eel Anguilla japonica and designated as anionic trypsin 1, had a molecular weight of 26,000 and an isoelectric point of 5.5. The amino acid composition of the enzyme was similar to that of bovine cationic trypsin as well as anionic trypsins from other species of fish. The enzyme was stable at pH 6 to 9 in the presence of calcium ions. Km and kcat values of the enzyme for N-tosyl-L-arginine methyl ester and N-tosyl-L-lysine methyl ester were quite similar to those of catfish anionic and bovine cationic trypsins.

摘要

从日本鳗鲡胰腺中分离出一种酶，命名为阴离子胰蛋白酶1，其分子量为26,000，等电点为5.5。该酶的氨基酸组成与牛阳离子胰蛋白酶以及其他鱼类的阴离子胰蛋白酶相似。在钙离子存在的情况下，该酶在pH 6至9时稳定。该酶对N-甲苯磺酰-L-精氨酸甲酯和N-甲苯磺酰-L-赖氨酸甲酯的Km和kcat值与鲶鱼阴离子胰蛋白酶和牛阳离子胰蛋白酶的非常相似。