Abstract
Pz-peptidase was purified from rat testis and rabbit muscle. Zinc was detectable in the rat enzyme. The activity of the enzyme from both species was slowly but completely abolished by EDTA and restored by Zn2+. Free thiol groups were also important for the catalytic activity of rat Pz-peptidase, as previously reported for the rabbit enzyme. We conclude that in both species Pz-peptidase has the characteristics of a thiol-dependent metallo-endopeptidase.
MeSH Terms
Amino Acid Sequence
Animals
Chromatography, DEAE-Cellulose
Chromatography, Gel
Chromatography, High Pressure Liquid
Dithiothreitol/pharmacology
Electrophoresis, Polyacrylamide Gel
Endopeptidases/isolation & purification,metabolism
Ethylmaleimide/pharmacology
Kinetics
Male
Metalloendopeptidases/metabolism
Molecular Sequence Data
Molecular Weight
Muscles/enzymology
Rabbits
Rats
Substrate Specificity
Chemicals
Endopeptidases
Metalloendopeptidases
thimet oligopeptidase
Ethylmaleimide
Dithiothreitol
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Tisljar U
Department of Biochemistry, Strangeways Research Laboratory, Cambridge, U.K.
Barrett A J
References (11)
11 references, click to expand
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