一种人脑啡肽降解氨肽酶的纯化及底物特性分析

Purification and substrate characterization of a human enkephalin-degrading aminopeptidase.

作者信息

Coletti-Previero M A, Mattras H, Descomps B, Previero A

出版信息

Biochim Biophys Acta. 1981 Jan 15;657(1):122-7. doi: 10.1016/0005-2744(81)90135-2.

Abstract

A 5000-fold purification of the enzyme responsible for the rapid inactivation of enkephalin in human blood has been achieved: this enzyme cleaves the N-terminal tyrosine from enkephalin and from short peptides provided their first amino acid is aromatic. The enzyme, an enkephalin-degrading aminopeptidase (alpha-aminoacyl-peptide hydrolase, EC 3.4.11.11), requires a free amino group on the substrate and has a maximum activity around pH 8. Its appearance molecular weight is in the range of 80 000-90 000 and an apparent Michaelis constant of 0.4 mM was determined.

摘要

已实现对人血液中负责脑啡肽快速失活的酶进行5000倍的纯化：该酶从脑啡肽和短肽上切割N端酪氨酸，前提是它们的第一个氨基酸是芳香族的。该酶是一种脑啡肽降解氨基肽酶（α-氨基酰基肽水解酶，EC 3.4.11.11），需要底物上有一个游离氨基，在pH 8左右具有最大活性。其表观分子量在80000 - 90000范围内，测定的表观米氏常数为0.4 mM。