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Partial purification and characterization of a proteoglycan‐degrading neutral protease from bovine epiphyseal cartilage
Author(s) -
Ehrlich Michael G.,
Armstrong Ann L.,
Mankin Henry J.
Publication year - 1984
Publication title -
journal of orthopaedic research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.041
H-Index - 155
eISSN - 1554-527X
pISSN - 0736-0266
DOI - 10.1002/jor.1100020203
Subject(s) - proteoglycan , proteases , cartilage , enzyme , biochemistry , protease , chemistry , chelation , calcification , neutral protease , extracellular matrix , biology , anatomy , medicine , inorganic chemistry
Degradation of the proteoglycan matrix is considered an essential step in the process of calcification in the growth plate. This laboratory has just described the presence of a protease in human growth plate cartilage that degrades proteoglycan at neutral pH. We report here the isolation, partial purification, and characterization of these proteoglycan‐degrading neutral proteases of bovine epiphyseal cartilage. It appears that there is more than a single enzyme active at neutral pH. These enzymes are of low molecular weight (below 30,000), poorly charged, and inhibited by metal chelating agents. Activity is best restored in the presence of zinc. This represents the first characterization of this important enzyme group.