Purification of pig synovial collagenase to high specific activity.
Biochem J, 1979/12/01;183(3):647-56.
PMID: 231970
Impact factor: 3.766
Abstract
1. Pig synovium in tissue culture secretes a specific collagenase in a latent form. 2. The latent enzyme was concentrated by (NH4)2SO4 precipitation and activated with 4-aminophenylmercuric acetate, and the active enzyme was purified by chromatography on Ultrogel AcA44, DEAE-cellulose, heparin-Sepharose and a zinc-chelate medium to a specific activity of 53 400 units/mg. of protein. 3. The enzyme was shown to be essentially homogeneous by polyacrylamide-gel electrophoresis. 4. The purified collagenase digested collagen to give the characteristic three-quarter and one-quarter pieces.
MeSH terms
Animals; Chromatography, Liquid; Collagen; Culture Techniques; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Methods; Microbial Collagenase; Phenylmercuric Acetate; Swine; Synovial Membrane
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