Biochemical and Immunochemical Characterization of Proteodermatan Sulfate from Calf Skin
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概要
- 論文の詳細を見る
A proteodermatan sulfate (PDS) was extracted from calf skin with 3M MgCl_2 in the presence of protease inhibitors and purified repeatedly by dimethylaminoethyl (DEAE)-cellulose chromatography. The average molecular weights were estimated to be 112000 for PDS and 56000 for core protein from chondroitinase ABC-treated PDS in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Unsaturated disaccharide of the glycosaminoglycan side chain (molecular weight=20000) of PDS was found to be mainly composed (96.8%) of ΔDi-4S [2-acetamido-2-deoxy-3-O-(β-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose] as determined by high-performance liquid chromatography (HPLC).Affinity-purified rat antibody rat against the core protein of PDS reacted specifically with PDS, but there was no cross-reaction with extracellular molecules such as A1-D1 proteoglycan from cartilage, fibronectin, laminin, and types I, II, III and IV collagens. Furthermore, high specificity of the antibdy to PDS was also observed by immunoblotting after SDS-PAGE. Indirect immunofluorescence straining of anti-core protein antibody in tissues generally appeared along with interstitial collagen (types I, II and III). However, the fine reticular fiber composed to types I and III collagens in liver was not stained.On the basis of these findings and of biochemical characterization of PDS, it is postulated that PDS possibly contributes to promotion of collagen fibrillogenesis and deposition in the extracellular matrix in vivo.
- 公益社団法人日本薬学会の論文
- 1988-12-25
著者
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小野寺 敏
Department of Clinical and Biomedical Sciences, Showa Pharmaceutical University
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小野寺 敏
Department Of Clinical Chemistry Showa College Of Pharmaceutical Sciences
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- Biochemical and Immunochemical Characterization of Proteodermatan Sulfate from Calf Skin