Cartilage proteoglycan aggregates. The link protein and proteoglycan amino-terminal globular domains have similar structures.
نویسندگان
چکیده
منابع مشابه
The role of link-protein in the structure of cartilage proteoglycan aggregates.
Proteoglycan fractions were prepared from pig laryngeal cartilage. The effect of link-protein on the properties of proteoglycan-hyaluronate aggregates was examined by viscometry and analytical ultracentrifugation. Aggregates containing link-protein were more stable than link-free aggregates at neutral pH, at temperatures up to 50 degrees C and in urea (up to 4.0M). Oligosaccharides of hyalurona...
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Aggregated proteoglycans (70% aggregated), isolated from the Swarm rat chondrosarcoma by extraction with 4 M guanidinium chloride in the presence of protease inhibitors and purified by centrifugation in an associative cesium chloride gradient, were separated into the component parts by centrifugation in a dissociative cesium chloride gradient. The gradient was cut into five equal fractions. The...
متن کاملA study of the interaction between cartilage proteoglycan and link protein.
The interaction between proteoglycan and link protein extracted from bovine articular cartilage (15-18-month-old animals) was investigated in 0.5 M-guanidinium chloride. The proteoglycans, radiolabelled as the aggregate (A1 fraction), were fractionated by two 'dissociative' density-gradient centrifugations (A1D1D1) followed by a rate-zonal centrifugation (S1) to yield an A1D1D1S1 preparation. A...
متن کاملHyaluronic acid in cartilage and proteoglycan aggregation.
1. Dissociation of purified proteoglycan aggregates was shown to release an interacting component of buoyant density higher than that of the glycoprotein-link fraction of Hascall & Sajdera (1969). 2. This component, which produced an increase in hydrodynamic size of proteoglycans on gel chromatography, was isolated by ECTEOLA-cellulose ion-exchange chromatography and identified as hyaluronic ac...
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Glucosamine (GlcN) and glucosamine sulfate (GS) have been used to treat the patients with osteoarthritis (OA) as a disease-modifying agent. Previous in vitro studies have focused on the effects of GlcN or GS on cartilage metabolism, whereas in vivo studies have investigated their potential for the treatment of OA. Although these results have raised promises of the disease-modifying effects of G...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)45445-2