Affordable Access

K-13, a novel inhibitor of angiotensin I converting enzyme produced by Micromonospora halophytica subsp. exilisia. I. Fermentation, isolation and biological properties.

Authors
  • Kase, H
  • Kaneko, M
  • Yamada, K
Type
Published Article
Journal
The Journal of antibiotics
Publication Date
Apr 01, 1987
Volume
40
Issue
4
Pages
450–454
Identifiers
PMID: 3034844
Source
Medline
License
Unknown

Abstract

A novel inhibitor of angiotensin I converting enzyme (ACE), designated K-13, was isolated from the culture broth of Micromonospora halophytica subsp. exilisia K-13. K-13 inhibited ACE non-competitively when hippuryl-L-histidyl-L-leucine was used as a substrate. The inhibition constant (Ki) was 0.349 microM. K-13 hardly inhibited carboxypeptidase A, trypsin, alpha-chymotrypsin, leucine aminopeptidase, and aminopeptidase B even at a level of 61 microM. When K-13 was administered intravenously to rats, it inhibited the pressor response to angiotensin I.

Report this publication

Statistics

Seen <100 times