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Activity of Pz-peptidase and endo-oligopeptidase are due to the same enzyme
U Tisljar1, A C de Camargo, C A da Costa
1Biochemistry Department, Strangeways Research Laboratory, Cambridge, United Kingdom.
Biochemical and Biophysical Research Communications
|August 15, 1989
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.