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PMID: 2930500 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Purification of the neutral proteoglycan-degrading metalloproteinase from human articular cartilage tissue and its identification as stromelysin matrix metalloproteinase-3.

The Biochemical journal ·Vol. 258 ·No. 1 ·1989-02-15 ·Pages 115-9

Gunja-Smith Z, Nagase H, Woessner JF

Abstract

The 'neutral' proteoglycan-degrading metalloproteinase of human articular cartilage was purified 3,500-fold by use of an anti-(matrix metalloproteinase-3) immunoglobulin G affinity column. Molecular masses of the latent and multiple active forms and specificity of action on casein, transferrin, gelatin and fibronectin were identical with those of authentic stromelysin (matrix metalloproteinase-3) from cultured human rheumatoid synovial fibroblasts. The optimum pH of this proteinase on proteoglycan monomer was pH 5.5, and on Azocoll, 6.2; digestion of fibronectin and gelatin was more extensive at pH 5.5 than at 7.5.

MeSH Terms
Cartilage, Articular/analysis Humans Hydrogen-Ion Concentration Matrix Metalloproteinase 3 Metalloendopeptidases/isolation & purification,metabolism Proteoglycans/metabolism Substrate Specificity
Chemicals
Proteoglycans Metalloendopeptidases Matrix Metalloproteinase 3
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Gunja-Smith Z
Department of Medicine, University of Miami School of Medicine, FL 33101.
Nagase H
Woessner J F
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22 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1989-02-15
Pages
115-9
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1138331
Subset
IM
Grants
NIAMS NIH HHS · AR-16940 · United States
NIAMS NIH HHS · AR-39189 · United States
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