Activity of Pz-peptidase and endo-oligopeptidase are due to the same enzyme

Biochem Biophys Res Commun. 1989 Aug 15;162(3):1460-4. doi: 10.1016/0006-291x(89)90838-3.

Abstract

During purification of endo-oligopeptidase from rabbit heart, activities cleaving bradykinin, a substrate of endo-oligopeptidase, and Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp), a substrate of Pz-peptidase, were found in the same fractions. The hydrolysis of both substrates was inhibited by antisera against endo-oligo-peptidase and Pz-peptidase, and reversibly inhibited by 1, 10-phenanthroline. The purified enzyme hydrolysed Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys, another substrate of Pz-peptidase. Purified Pz-peptidase from rabbit muscle degraded bradykinin and was inhibited by an antiserum against endo-oligopeptidase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chromatography
  • Cysteine Endopeptidases / metabolism*
  • Cysteine Proteinase Inhibitors
  • Endopeptidases / metabolism*
  • Immunologic Techniques
  • Metalloendopeptidases*
  • Phenanthrolines / pharmacology
  • Protease Inhibitors
  • Rabbits

Substances

  • Cysteine Proteinase Inhibitors
  • Phenanthrolines
  • Protease Inhibitors
  • Endopeptidases
  • Cysteine Endopeptidases
  • Metalloendopeptidases
  • thimet oligopeptidase
  • 1,10-phenanthroline