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Further characterization of a neutral metalloprotease isolated from human articular cartilage

✍ Scribed by Dr. Asher I. Sapolsky; David S. Howell

Publisher
John Wiley and Sons
Year
1982
Tongue
English
Weight
746 KB
Volume
25
Category
Article
ISSN
0004-3591

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✦ Synopsis

Abstract

The neutral metalloprotease extracted from 1,200 gm of human articular cartilage was purified 1,400‐ to 2,400‐fold by diethylaminoethyl‐ and carboxymethyl‐Sephadex chromatography. Disc electrophoresis and an isoelectric focusing method resolved the neutral enzyme activity into 4 bands. All bands had a similar amino acid analysis and a similar molecular weight by sodium dodecylsulfate electrophoresis and gel filtration: 24,000–27,000 daltons. The enzyme degraded proteoglycan subunit and proteoglycan aggregate to products with a sedimentation coefficient of 3S, but at low dilutions the enzyme produced 19.3S fragments. It is postulated that this protease may contribute to the development of osteoarthritis from within the cartilage matrix.

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