Jan 1, 1984

Partial purification and characterization of a proteoglycan-degrading neutral protease from bovine epiphyseal cartilage

Journal of Orthopaedic Research : Official Publication of the Orthopaedic Research Society
M G EhrlichH J Mankin

Abstract

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.

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Citations

Mentioned in this Paper

Enzymes, antithrombotic
Proteoglycan
Bos taurus
Chelating Agents
Endopeptidases
Proteolytic Enzyme
Viscosity
Epiphysis of Bone
Enzymes for Treatment of Wounds and Ulcers
Proteoglycan-degrading neutral proteases

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