IDENTIFICATION AND CHARACTERIZATION OF 2 DISTINCT KYOTORPHIN-HYDROLYZING ENZYMES IN RAT-BRAIN

被引：11

作者：

AKASAKI, K

NAKAMURA, A

SHIOMI, H

TSUJI, H

机构：

[1] Faculty of Pharmacy and Pharmaceutical Sciencies, Fukuyama University, Fukuyama, Hiroshima

来源：

NEUROPEPTIDES | 1991年 / 20卷 / 02期

关键词：

D O I：

10.1016/0143-4179(91)90059-R

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

We identified and characterized two kyotorphin-hydrolyzing peptidases (KTPases) in a soluble fraction of rat brain. When the soluble fraction was chromatographed with DEAE-Sephacel, the enzyme activity was resolved into two peaks, which were designated as KTPases I and II in their order of elution. KTPases I and II accounted for 95% and 5% of the KTPase activity in the soluble fraction, respectively. KTPases I and II hydrolyzed kyotorphin with K(m) values of 22-mu-M and 110-mu-M, respectively. By gel filtration, M(r) values of KTPases I and II were determined to be 55 000 and 98 000, respectively. Immunological analyses of KTPase II with an anti-enkephalin aminopeptidase antibody indicated that KTPase II was identical to an enkephalin aminopeptidase with M(r) = 98 000. However, KTPase I was a novel peptidase responsible for the major kyotorphin-degrading activity in the soluble fraction of rat brain.

引用

页码：103 / 107

页数：5

共 17 条

[1]

Cuatrecasas P., 1971, METHOD ENZYMOL, V22, P345

[2] PURIFICATION AND CHARACTERIZATION OF ARYLAMIDASE FROM MONKEY BRAIN [J].