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Cleavage of des-Arg9-bradykinin by angiotensin I-converting enzyme from pig kidney cortex

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Fast and very slow hydrolyses of des-Arg9-bradykinin and angiotensin II by angiotensin I-converting enzyme were detected by high performance liquid chromatography. The Michaelis constants of the enzyme, Km values, for des-Arg9-bradykinin and bradykinin were found to be 0.24 mM and 4.4 μM, and the maximum velocities, Vmax values (μmol·min−1·mg protein−1) for these compounds to be 3.24 and 0.34, respectively. The enzyme also hydrolyzed Z-Gly-Pro-Gly-Gly-Pro-Ala to a tripeptide that was identified as dansyl-Gly-Pro-Ala by TLC on polyamide. These observations show that the enzyme hydrolyzes the peptides at the bond before the prolyl residue in the penultimate position.

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Acknowledgments. We thank Dr Kinzo Nagasawa of Kitasato University for encouragement in this work and Dr Ervin G. Erdös, University of Texas, Health Science Center, Dallas, for valuable discussion and suggestions.

Abbreviations used: Z, carbobenzoxy; Bz, benzoyl; ACE, angiotensin I-converting enzyme; BK, bradykinin; HPLC, high performance liquid chromatography.

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Oshima, G., Hiraga, Y., Shirono, K. et al. Cleavage of des-Arg9-bradykinin by angiotensin I-converting enzyme from pig kidney cortex. Experientia 41, 325–328 (1985). https://doi.org/10.1007/BF02004493

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