兔脑硫醇激活的内肽酶。缓激肽和激肽原的水解。

Rabbit brain thiol-activated endopeptidase. Hydrolysis of bradykinin and kininogen.

作者信息

Oliveira E B, Martins A R, Camargo A C

出版信息

Gen Pharmacol. 1976 Aug;7(2-3):159-61. doi: 10.1016/0306-3623(76)90054-9.

Abstract

A neutral brain endopeptidase which hydrolyzes bradykinin (Arg1-Pro2-Pro3-Gly4-Phe5-Ser6-Pro7-Phe8-Arg9) at the Phe5-Ser6 peptide bond was activated about 10 times by dithiothreitol. The preferential specificity of the enzyme for small peptides was suggested on the basis of the absence of activity toward a bradykinin-related protein such as S-carboxymethylated plasma kininogen.

摘要

一种中性脑内肽酶可在苯丙氨酸5 - 丝氨酸6肽键处水解缓激肽（精氨酸1 - 脯氨酸2 - 脯氨酸3 - 甘氨酸4 - 苯丙氨酸5 - 丝氨酸6 - 脯氨酸7 - 苯丙氨酸8 - 精氨酸9），该酶被二硫苏糖醇激活约10倍。基于对一种与缓激肽相关的蛋白质（如S - 羧甲基化血浆激肽原）无活性，提示该酶对小肽具有优先特异性。