title: Purification of pig synovial collagenase to high specific activity.
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: D000818:Animals; D002853:Chromatography, Liquid; D003094:Collagen / Q000378:metabolism; D046508:Culture Techniques; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D008722:Methods; D003012:Microbial Collagenase / Q000302:isolation & purification* / Q000378:metabolism; D010662:Phenylmercuric Acetate / Q000031:analogs & derivatives / Q000494:pharmacology; D013552:Swine; D013583:Synovial Membrane / Q000201:enzymology*
chemical_list: D003094:Collagen; D003012:Microbial Collagenase; D010662:Phenylmercuric Acetate