070 Isolation and characterization of heparan sulphate proteoglycan from human articular cartilage
✍ Scribed by G. Stöcker; D. -C. Fischer; S. Handt; H. Greiling; H. -D. Haubeck
- Book ID
- 112293048
- Publisher
- Springer
- Year
- 1992
- Tongue
- English
- Weight
- 101 KB
- Volume
- 343
- Category
- Article
- ISSN
- 1618-2650
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Cartilage oligomeric matrix protein was purified in a native form from normal adult human articular cartilage. The key steps in the purification scheme were selective extraction with buffer containing EDTA, wheat germ agglutinin affinity chromatography, and removal of the related protein thrombospon
## 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.