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THE ABILITY OF VARIOUS INSULINS AND INSULIN FRAGMENTS TO INHIBIT THE ANGIOTENSIN I CONVERTING ENZYME
Author(s) -
Bing Jens,
Poulsen Knud,
Markussen Jan
Publication year - 1974
Publication title -
acta pathologica microbiologica scandinavica section a pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0365-4184
DOI - 10.1111/j.1699-0463.1974.tb00405.x
Subject(s) - insulin , angiotensin ii , chemistry , angiotensin converting enzyme , renin–angiotensin system , enzyme , medicine , radioimmunoassay , in vitro , endocrinology , in vivo , peptide , biochemistry , biology , receptor , microbiology and biotechnology , blood pressure
A variety of insulins and insulin fragments were shown to be active as inhibitors of angiotensin I converting enzyme from guinea pig plasma when tested in vitro. Angiotensin I was used as substrate and the consumption rate of angiotensin I as well as the generation rate of angiotensin II were measured by means of specific radioimmunoassays for angiotensin I and II. The B‐chain of insulin from different species possessed about the same inhibitory capacity as the whole insulin molecule. In an attempt to locate the active part of the sequence of the B‐chain, the five peptides which resulted from tryptic digestion of the duck insulin B‐chain were studied. They were, however, all active as inhibitors and on molar basis equal to or slightly more potent than the B‐chain and insulin. This demonstrates the unspecific nature of converting enzyme. Its affinity for insulin and its peptide fragments were, however, two to four orders of magnitude lower than it was for the most potent inhibitor described so far, the synthetic nonapeptide SQ 20.881. This difference was confirmed in in vivo experiments.