PMID: 40608Nov 9, 1979

Purification and properties of a collagen peptidase (PZ-peptidase) from rabbit serum

Biochimica Et Biophysica Acta
M NagelschmidtH Struck

Abstract

A peptidase cleaving a synthetic substrate for collagen peptidases, 4-phenylazobenzyloxcarbonyl-L-Pro-L-Leu-Gly-L-pro-D-Arg (designated as PZ-peptide) has been purified 1200-fold from rabbit serum and characterized. The enzyme preparation is free of collagenase and unspecific proteinase activity. The natural substrates are denatured collagen and collagen peptides. The peptidase has a molecular weight of 124 000 and an isoelectric point at pH 5.1. The pH dependence curve exhibits two maxima, one at pH 7.1 and the other at pH 7.9. The enzymic reaction is completely inhibited by Zn2+ and to a slower degree by Hg2+, Mn2+ and p-hydroxymercuribenzoate. It is not affected by EDTA and KCN but totally blocked by o-phenanthroline. Phenylmethylsulfonylfluoride is completely inhibitory and points to a serine residue in the active site.

References

Jan 1, 1984·Neurochemistry International·T ChikumaT Kato
Oct 20, 2005·Journal of Bioscience and Bioengineering·K AkiyamaR Takata
Oct 1, 1989·Archives of Biochemistry and Biophysics·U Tisljar, A J Barrett
Apr 15, 1988·Biochemical and Biophysical Research Communications·E L RuggG Cramb
Jan 1, 1982·Research in Experimental Medicine. Zeitschrift Für Die Gesamte Experimentelle Medizin Einschliesslich Experimenteller Chirurgie·R BirnbaumH Struck

Citations

Oct 1, 1966·Biochemistry·Y NagaiJ Gross

Related Concepts

4-hydroxymercuribenzoate
SDS-PAGE
Peptide Hydrolases
Oligopeptides
Proteolytic Enzyme
Enzyme agent
Chinchilla Rabbits
1,10-phenanthroline
Substrate Specificity
Collagenase-Like Peptidase

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