DEGRADATION OF BRADYKININ BY ISOLATED NEUTRAL ENDOPEPTIDASES OF BRAIN AND PITUITARY

被引：33

作者：

WILK, S

ORLOWSKI, M

机构：

[1] Department of Pharmacology, New York, NY 10029, Mount Sinai School Medicine Fifth Ave. and

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 90卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0006-291X(79)91581-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The degradation of bradykinin by a highly purified preparation of rabbit brain prolyl endopeptidase and by an apparently homogeneous preparation of a bovine pituitary cation-sensitive neutral endopeptidase was studied. Peptide fragments were separated and isolated by high performance liquid chromatography and identified by amino acid analysis. Prolyl endopeptidase rapidly cleaves bradykinin at the Pro7-Phe8 bond. A slower cleavage also occurs at the Pro3-Gly4 bond. Cation-sensitive neutral endopeptidase splits bradykinin at the Phe5-Ser6 bond. These enzymes may participate in the regulation of brain concentrations of bradykinin. © 1979.

引用

页码：1 / 6

页数：6

共 16 条

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