Purification of pig synovial collagenase to high specific activity
- 1 December 1979
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 183 (3) , 647-656
- https://doi.org/10.1042/bj1830647
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.This publication has 30 references indexed in Scilit:
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