A DISTINCT PEPTIDYL DIPEPTIDASE THAT DEGRADES ENKEPHALIN - EXCEPTIONALLY HIGH-ACTIVITY IN RABBIT KIDNEY

被引：27
作者：
BENUCK, M [1 ]
BERG, MJ [1 ]
MARKS, N [1 ]
机构：
[1] ROCKLAND RES INST, CTR NEUROCHEM, WARDS ISL, NY 10035 USA
来源：
LIFE SCIENCES | 1981年 / 28卷 / 23期
关键词：
D O I：
10.1016/0024-3205(81)90722-0
中图分类号：
R-3 [医学研究方法]; R3 [基础医学];
学科分类号：
1001 ;
摘要：
Peptidyl dipeptidase activity distinct from the angiotensin converting enzyme (EC 3.4.15.1) was isolated from membrane fractions of rabbit kidney and lung. The enzyme cleaved Leu-enkephalin at the Gly-Phe bond, releasing Tyr-Gly-Gly and Phe-Leu, and also acted on bradykinin releasing the terminal dipeptide Phe-Arg. In contrast to the converting enzyme, this peptidyl dipeptidase did not act on angiotensin I, or on hippuryl His-Leu, nor was it inhibited by captopril (SQ 14225) or by SQ 20881 [teprotide]. Kinetic studies indicated a Km for the kidney enzyme of 80 .mu.M with Leu-enkephalin as a substrate. Evidently more than 1 enzyme is present in membrane preparations of lung and kidney inactivating enkephalin; these enzymes may be involved in the peripheral actions of opiate and related peptides.
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页码：2643 / 2650
页数：8
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