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- W2116786132 abstract "guanidinium chloride in the presence of protease inhibitors and purified by centrifugation in an associative cesium chlo- ride gradient, were separated into the component parts by centrifugation in a dissociative cesium chloride gradient. The gradient was cut into five equal fractions. The bottom fraction contained 98% of the chondroitin sulfate and 84% of the protein of the aggregate preparation. Sedimentation equilibrium studies on the protein core of this fraction, isolated by column chromatography from chondroitinase ABC digests, suggest that its molecular weight is 2.0 x lo” to 2.2 x 1W. The intermediate fractions of lower buoyant den- sities contained hyaluronic acid (0.8% of the total weight of the aggregated preparations) and proteoglycan monomers with fewer chondroitin sulfate chains relative to the protein core than in the bottom fraction. The top fraction, in addi- tion to proteoglycans, contained a link protein. The link protein was separated from the proteoglycans by chroma- tography on Sephadex G-200 in the presence of 4" @default.
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- W2116786132 date "1977-09-01" @default.
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- W2116786132 title "The link protein in proteoglycan aggregates from the Swarm rat chondrosarcoma." @default.
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- W2116786132 doi "https://doi.org/10.1016/s0021-9258(17)39982-9" @default.
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