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 l(R)-l-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. © 1986, JAPAN ANTIBIOTICS RESEARCH ASSOCIATION. All rights reserved.
CITATION STYLE
Yamato, M., Koguchi, T., Okachi, R., Yamada, K., Nakayama, K., Kase, H., … Shuto, K. (1986). K-26, a novel inhibitor of angiotensin I converting enzyme produced by an actinomycete K-26. The Journal of Antibiotics, 39(1), 44–52. https://doi.org/10.7164/antibiotics.39.44
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