Some properties of latent collagenase from human synovial fluid

Wize, J, Knauper, V ORCID: https://orcid.org/0000-0002-3965-9924 and Tschesche, H 1990. Some properties of latent collagenase from human synovial fluid. Acta Biochimica Polonica 37 (1) , pp. 201-206.

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Abstract

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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Polskie Towarzystwo Biochemiczne / Acta Biochimica Polonica
ISSN:	0001-527X
Last Modified:	31 Aug 2023 09:15
URI:	https://orca.cardiff.ac.uk/id/eprint/161652

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