Literature DB >> 189024

The metalloenzymic nature of collagenase-like peptidase of the rat testis.

J Lukac, E Koren.   

Abstract

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.

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Year:  1977        PMID: 189024     DOI: 10.1530/jrf.0.0490095

Source DB:  PubMed          Journal:  J Reprod Fertil        ISSN: 0022-4251


  3 in total

1.  The activities of 'Pz-peptidase' and 'endopeptidase 24.15' are due to a single enzyme.

Authors:  A J Barrett; U Tisljar
Journal:  Biochem J       Date:  1989-08-01       Impact factor: 3.857

2.  Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase.

Authors:  A J Barrett; M A Brown
Journal:  Biochem J       Date:  1990-11-01       Impact factor: 3.857

3.  Thiol-dependent metallo-endopeptidase characteristics of Pz-peptidase in rat and rabbit.

Authors:  U Tisljar; A J Barrett
Journal:  Biochem J       Date:  1990-04-15       Impact factor: 3.857

  3 in total

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