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Vasopeptides pp 149-153 | Cite as

Identity of Kininase II with an Angiotensin I Converting Enzyme

  • R. Igic
  • K. Sorrells
  • T. Nakajima
  • E. G. Erdös
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 21)

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.

Keywords

Perfusion Fluid Glycine Derivative High Voltage Electrophoresis Hypotensive Peptide Label Angiotensin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    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.Google Scholar
  2. 2.
    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.Google Scholar
  3. 3.
    Igic, R., Erdös, E.G., Yeh, H.S.Y., and Sorrells, K. The angiotensin I converting enzyme of the lung. Circul. Res. In press.Google Scholar

Copyright information

© Plenum Press, New York 1972

Authors and Affiliations

  • R. Igic
    • 1
  • K. Sorrells
    • 1
  • T. Nakajima
    • 1
  • E. G. Erdös
    • 1
  1. 1.Department of PharmacologyUniversity of Oklahoma School of MedicineOklahoma CityUSA

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