The metalloenzymic nature of collagenase-like peptidase of the rat testis.
Collagenase-like peptidase, an enzyme degrading synthetic collagenase substrate (PZ-pentapeptide), was purified from rat testes and its properties were examined. Its activity was strongly inhibited by chelating agents, such as EDTA and 1,10-phenanthroline. By chelation and exhaustive dialysis it was possible to obtain this enzyme in its inactive, metal-free form. The activity of the metal-free enzyme was partly recovered by treatment with zinc or manganese ions, while a combined zinc and manganese treatment resulted in complete recovery of enzyme activity.
D000818:Animals; D002614:Chelating Agents; D003956:Dialysis; D004492:Edetic Acid; D004573:Electrolytes; D010450:Endopeptidases / Q000032:analysis / Q000302:isolation & purification*; D008297:Male; D003012:Microbial Collagenase / Q000302:isolation & purification / Q000378:metabolism; D010455:Peptides; D051381:Rats; D013438:Sulfhydryl Compounds; D013737:Testis / Q000201:enzymology*
D002614:Chelating Agents; D004573:Electrolytes; D010455:Peptides; D013438:Sulfhydryl Compounds; D004492:Edetic Acid; D010450:Endopeptidases; D003012:Microbial Collagenase