Studies on the hydrolysis of bradykinin by angiotensin-converting enzyme (kininase II) |
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| Authors: | F. E. Dorer J. M. Stewart J. W. Ryan |
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| Affiliation: | (1) Hypertension Research Laboratory, Veterans Administration Hospital andDepartment of Biochemistry, Case Western Reserve University, 44106 Cleveland, Ohio, USA;(2) Department of Biochemistry, University of Colorado Medical Center, 80220 Denver, Colorado, USA;(3) Department of Medicine, University of Miami School of Medicine, 33152 Miami, Florida, USA |
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| Abstract: | Summary Arg-Pro-Pro-Gly-Phe, the N-terminal pentapeptide of bradykinin, is not an inhibitor of angiotensin-converting enzyme and is not hydrolyzed by the enzyme. Arg-Pro-Pro, the N-terminal tripeptide is a relatively potent (IC50=2.3×106 M) inhibitor but its higher homolog, Gly-Arg-Met-Lys-Arg-Pro-Pro is not an inhibitor of angiotensin-converting enzyme.This work was supported in part by grants from the US Public Health Service (HL 18415, HL 15691, HL 19764) and the John A. Hartford Foundation, Inc., and by the Medical Research Service of the Veterans Administration. |
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