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Collagenase Studies in bones of guinea pigs *
Author(s) -
Heard Sam Bryan
Publication year - 1976
Publication title -
journal of oral pathology and medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.887
H-Index - 83
eISSN - 1600-0714
pISSN - 0904-2512
DOI - 10.1111/j.1600-0714.1976.tb01754.x
Subject(s) - collagenase , guinea pig , proteases , enzyme , biochemistry , chemistry , microbiology and biotechnology , biology , endocrinology
. A specific collagenase has been demonstrated in culture fluids of guinea pig bones. Based on the acrylamide gel eleclrophoretic pattern, the mechanism of action of guinea pig bone collagenase appears similar to other known vertebrate collagenases. Two peaks of enzymatic activity were found upon assay of fractions from gel chromatography, corresponding to molecular weights in the range of 137,000 daltons and 29,000 daltons. The enzyme is inhibited by cysteine and EDTA. Alpha 2 ‐macroglobulin is a much stronger inhibitor of the collagenase than alpha 1 ‐antitrypsin. Activation studies suggested the presence of a proenzyme to guinea pig bone collagenase that was converted to an active enzyme by proteases present in the culture fluid.