Abstract
Prolylcarboxypeptidase (PCP) was discovered in the kidney by Yang, Erdös, and associates (1–3). Because the enzyme cleaved the Pro7-Phe8 bond in angiotensin II, it was called angiotensinase C. PCP was soon found, however, to hydrolyze many other peptide substrates with a general structure of R1-Pro-R2-OH. Here R1 can be either a blocking group, a dansyl group, another amino acid, or a peptide. R2 is an aromatic or aliphatic amino acid with a free carboxyl group. Substrates in which proline is replaced by another amino acid are not cleaved. The enzyme is most active at an acid pH. It is inhibited by diisopropyl phosphorofluoridate (DFP), and it differs from catheptic enzymes. In the body (2, 4), PCP occurs in lysosomal fractions of the kidney and of human leukocytes, and elsewhere.
This work was supported in part by Grants HE-08764 and 5T01-HE-05859 from NIH, USPHS, and by the Office of Naval Research Contract N00014-68-A-0496 and N00014-69-A00385.
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References
Yang, H.Y.T., E.G. Erdös, and T.S. Chiang. New enzymatic route for the inactivation of angiotensin. Nature (London) 218: 1224, 1968.
Yang, H.Y.T., E.G. Erdös, T.S. Cniang, T.A. Jenssen, and J.G. Rodgers. Characterization of an enzyme that inactivates angiotensin II (angiotensinase C). Biochem. Pharmacol. 19: 1201, 1970.
Yang, H.Y.T., and E.G. Erdös. In: Immunopathology of Inflammation, edited by B.K. Forscher and J.C. Houck. Amsterdam: Excerpta Medica, 1971, p. 146.
Sorrells, K., and E.G. Erdös. Prolylearboxypeptidase (angiotensinase C) in subcellular particles of leukocytes. Fed. Proc. 30: 600, 1971.
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© 1972 Plenum Press, New York
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Sorrells, K., Erdös, E.G. (1972). Prolylcarboxypeptidase in Biological Fluids. In: Hinshaw, L.B., Cox, B.G. (eds) The Fundamental Mechanisms of Shock. Advances in Experimental Medicine and Biology, vol 23. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9014-9_36
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DOI: https://doi.org/10.1007/978-1-4615-9014-9_36
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