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PMID: 231970 Published · ppublish English Journal Article

Purification of pig synovial collagenase to high specific activity.

The Biochemical journal ·Vol. 183 ·No. 3 ·1979-12-01 ·Pages 647-56

Cawston TE, Tyler JA

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/metabolism Culture Techniques Electrophoresis, Polyacrylamide Gel Enzyme Activation/drug effects Methods Microbial Collagenase/isolation & purification,metabolism Phenylmercuric Acetate/analogs & derivatives,pharmacology Swine Synovial Membrane/enzymology
Chemicals
Collagen Microbial Collagenase Phenylmercuric Acetate
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Cawston T E
Tyler J A
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29 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1979-12-01
Pages
647-56
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1161646
Subset
IM
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