Biological properties of angiotensin-converting enzyme inhibitor derived from tuna muscle.
- 1 January 1989
- journal article
- research article
- Published by Pharmaceutical Society of Japan in Journal of Pharmacobio-Dynamics
- Vol. 12 (9) , 566-571
- https://doi.org/10.1248/bpb1978.12.566
Abstract
A novel inhibitor of angiotensin-converting enzyme (ACE) derived from tuna muscle, Pro-Thr-His-Ile-Lys-Trp-Gly-Asp (tuna AI), was chemically synthesized, and its biological properties were investigated. Synthetic tuna AI was found to be chemically and biologically indistinguishable from the native one. Tuna AI inhibited rabbit lung ACE non-competitively with Ki values of 1.7 and 5.7 .mu.M with substrates, hippuryl-L-histidyl-L-leucine and angiotensin I, respectively. This peptide (5.3 .mu.M) also doubled the effect of bradykinin in the contraction of isolated guinea pig ileum. The peptide did not show zinc chelating activity and carboxypeptidase A inhibitory activity. Thus, tuna AI was found to be a unique ACE inhibitory peptide with non-competitive manner, differing from many naturally occurring peptide ACE-inhibitors.This publication has 9 references indexed in Scilit:
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