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. 1981 Nov;78(11):6623–6627. doi: 10.1073/pnas.78.11.6623

Purification of a membrane-bound metalloendopeptidase from porcine kidney that degrades peptide hormones.

R A Mumford, P A Pierzchala, A W Strauss, M Zimmerman
PMCID: PMC349101  PMID: 7031658

Abstract

A porcine kidney microsomal metalloendopeptidase has been enriched 3900-fold. Gel filtration on a calibrated Toyo-Soda G-3000 SW column indicated an appropriate molecular weight for the endopeptidase of 88,000 +/- 2000. The purified enzyme is inhibited by a number of synthetic inhibitors of thermolysin. The endopeptidase hydrolyzes the succinyl (Suc)-containing fluorogenic peptide substrate Suc-Ala-Ala-Phe-(7-amino-4-methylcoumarin) at the Ala-Phe position with a Km of 2.9 X 10(-4) M. The endopeptidase also hydrolyzes a variety of peptides including corticotropin, substance P, angiotensin I and II, neurotensin, somatostatin, bradykinin, and the renin tetradecapeptide substrate. The endopeptidase hydrolyzes both [Leu]- and [Met]enkephalin at the Gly-Phe bond.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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