Activity of Pz-peptidase and endo-oligopeptidase are due to the same enzyme.
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.
Tisljar
U
U
Biochemistry Department, Strangeways Research Laboratory, Cambridge, United Kingdom.
de Camargo
A C
AC
da Costa
C A
CA
Barrett
A J
AJ
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
D015853:Cysteine Proteinase Inhibitors; D010618:Phenanthrolines; D011480:Protease Inhibitors; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D008666:Metalloendopeptidases; C022510:thimet oligopeptidase; C025205:1,10-phenanthroline