Some properties of latent collagenase from human synovial fluid.
Latent collagenase has been isolated in pure form from the rheumatoid synovial fluid. The final preparation, activated by trypsin, yielded a collagenase of specific activity 2,227 units/mg. Electrophoresis in sodium dodecyl sulfate polyacrylamide gels revealed a protein doublet of 54 and 50 kDa. Trypsin or HgCl2 activation resulted in disappearance of the doublet and emergence of a new doublet of 47 and 43 kDa. The latent collagenase could also be activated by leucocyte cathepsin G or plasmin. Neither the latent nor the active collagenase from synovial fluid showed any cross-reactivity with the antibodies against leucocyte collagenase. The trypsin activated collagenase degraded collagen type I, II, III giving typical cleavage products but did not degrade type IV and V collagen.
Wize
J
J
Department of Biochemistry, Institute of Rheumatology, Warszawa, Poland.
Knäuper
V
V
Tschesche
H
H
D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D008627:Mercuric Chloride / Q000494:pharmacology; D003012:Microbial Collagenase / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D013582:Synovial Fluid / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D046911:Macromolecular Substances; D008627:Mercuric Chloride; D014357:Trypsin; D003012:Microbial Collagenase