| Literature DB >> 3005218 |
M Yamato, T Koguchi, R Okachi, K Yamada, K Nakayama, H Kase, A Karasawa, K Shuto.
Abstract
A novel inhibitor of angiotensin I converting enzyme (ACE), designated K-26, was isolated from the broth filtrate of an actiomycete K-26. K-26 is a water soluble, acidic peptide composed of an equal mol of L-isoleucine, L-tyrosine and 1(R)-1-amino-2-(4-hydroxyphenyl)-ethylphosphonic acid. The IC50 of K-26 for ACE inhibition was 6.7 ng/ml when hippuryl-L-histidyl-L-leucine was used as a substrate of ACE. K-26 possesses hypotensive activity in vivo.Entities:
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Year: 1986 PMID: 3005218 DOI: 10.7164/antibiotics.39.44
Source DB: PubMed Journal: J Antibiot (Tokyo) ISSN: 0021-8820 Impact factor: 2.649