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-Lhistidyl-L-leucine was used as a substrate of ACE. K-26 possesses hypotensive activity in vivo.Angiotensin I converting enzyme (ACE) has been found to play a critical role in the regulation of blood pressure in man and animals.Ever since the discovery of captoprill1) a specific inhibitor of ACE, and its successful application to the therapy of hypertension, attempts have been made to develop
A new antibiotic, CV-1, was isolated from the culture broth of a Streptomyces sp. by various chromatographies.CV-1 showed antibacterial activity against Escherichia coli in cooperation with spiramycin, a macrolide antibiotic.The mode of action of CV-1 seemed to be the inhibition of lipopolysaccharide synthesis. 723 In the course of our screening program for new antibiotics, wefound a new antibiotic, CV-1, from Streptomyces strain CO-1. CV-1 exhibited cooperative antibacterial activity with spiramycin against Escherichia coli. Spiramycin alone, was not effective against E. coli. In this paper, the fermentation, isolation, antibacterial activity and mode of action of CV-1are presented. Details of the physico-chemical properties and structure determination of CV-1 will be given in the following paper.1}
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