title: Activity of Pz-peptidase and endo-oligopeptidase are due to the same enzyme.
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.
authors.affiliation: Biochemistry Department, Strangeways Research Laboratory, Cambridge, United Kingdom.
authors.forename: U
authors.initials: U
authors.lastname: Tisljar
authors.forename: A C
authors.initials: AC
authors.lastname: de Camargo
authors.forename: C A
authors.initials: CA
authors.lastname: da Costa
authors.forename: A J
authors.initials: AJ
authors.lastname: Barrett
mesh_terms: D000818:Animals; D002845:Chromatography; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors; D010450:Endopeptidases / Q000378:metabolism*; D007158:Immunologic Techniques; D008666:Metalloendopeptidases; D010618:Phenanthrolines / Q000494:pharmacology; D011480:Protease Inhibitors; D011817:Rabbits
chemical_list: D015853:Cysteine Proteinase Inhibitors; D010618:Phenanthrolines; D011480:Protease Inhibitors; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D008666:Metalloendopeptidases; C022510:thimet oligopeptidase; C025205:1,10-phenanthroline