Abstract
Blood and tissues contain various enzymes that hydrolyze bradykinin. Among the ones we characterized were a prolidase (imidopeptidase), a carboxypeptidase-type enzyme (carboxypeptidase N; kininase I) and a dipeptide hydrolase (kininase II; DH). Carboxypeptidase N inactivates kinins by removing the C-terminal arginine, while kininase II liberates the dipeptide Phe-Arg from the same end.
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References
Erdös, E.G., and Yang, H.Y.T. Kininases. In Bradykinin, Kallidin and Kallikrein. Handbook of Experim. Pharmacol., Vo l. 25, ed. by Erdös, E.G., Heidelberg, Springer-Verlag, Pg. 289.
Yang, H.Y.T., Erdös, E.G., and Levin, Y. Characterization of a dipeptide hydrolase (kininase II; angiotensin I converting enzyme). J. Pharmacol. Exper. Therap. 117: 291, 1971.
Igic, R., Erdös, E.G., Yeh, H.S.Y., and Sorrells, K. The angiotensin I converting enzyme of the lung. Circul. Res. In press.
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© 1972 Plenum Press, New York
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Igic, R., Sorrells, K., Nakajima, T., Erdös, E.G. (1972). Identity of Kininase II with an Angiotensin I Converting Enzyme. In: Back, N., Sicuteri, F. (eds) Vasopeptides. Advances in Experimental Medicine and Biology, vol 21. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-7439-8_19
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DOI: https://doi.org/10.1007/978-1-4684-7439-8_19
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-7441-1
Online ISBN: 978-1-4684-7439-8
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