Separation of two PZ-peptidases from bovine dental follicle.
Two PZ-peptidases (EC 3.4.-) (A and B) cleaving a synthetic substrate for collagenase, 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu-Gly-L-Pro-D-Arg (PZ-peptide) have been separated from the particulate fraction of bovine dental follicle. PZ-peptidase A had a molecular weight of 220 000, an optimum pH at 8.0-8.5, and a Km value of 67 muM toward PZ-peptide at pH 7.1, whereas PZ-peptidase B had a molecular weight of 20 000, an optimum pH at 6.5-6.7, and a Km value of 400 muM toward PZ-peptide at pH 7.1. Two similar enzymes were also isolated from the soluble fraction. Since the pH-activity curve of the crude tissue preparations such as homogenate, microsomes and soluble supernatant had two peaks at 6.5-6.7 and 8.0-8.5, both PZ-peptidase A and B may exist in situ as two independent active enzymes.
D000818:Animals; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D008861:Microsomes / Q000201:enzymology; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D014083:Tooth Germ / Q000201:enzymology*
D007527:Isoenzymes; D046911:Macromolecular Substances; D010447:Peptide Hydrolases