Purification of a Noncollagenous High Molecular Weight Protein from Bovine Articular Cartilage
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概要
- 論文の詳細を見る
A noncollagenous high molecular weight protein (HMW) was isolated from bovine articular cartilage by CsCl density gradient centrifugation followed by DEAE-cellulose chromatography and gel filtration chromatography. The molecular weight was estimated to be 320 kDa and the reduced HMW had a molecular weight of 105 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The amino acid composition of HMW showed a high content of aspartic acid, but no hydroxylysine and hydroxyproline were detected, indicating that the protein was not a collagen. Affinity purified rabbit antibody against HMW reacted specifically with HMW, but there was no immunoreaction with cartilage-specific proteoglycan, type II collagen and type I collagen. HMW showed dose-dependent attachment to types I, II, III and V collagens. However, HMW did not bind to fibronectin, decorin and heparin. Furthermore, the binding of HMW to heat-denatured collagens was lower than native collagens. In these observation, HMW may be recognized the triple helix structure of collagen for the interaction.
- 公益社団法人日本薬学会の論文
- 1996-01-15
著者
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ONODERA Satoshi
Department of Clinical and Biomedical Sciences, Showa Pharmaceutical University
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TASHIRO Shinichi
Department of Clinical and Biomedical Science, Showa Pharmeceutical University
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Onodera Satoshi
Department Of Cinical And Biomedical Sciences Showa Pharmaceutical University
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KUBOKI Yoshinori
Department of Oral Biochemistry, School of Dentistry, Hokkaido University
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Kuboki Yoshinori
Department Of Biochemistry School Of Dentistry Hokkaido University
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Kuboki Yoshinori
Department Of Biochemistry Hokkaido University School Of Dentistry
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Tashiro Shinichi
Department Of Clinical And Biomedical Sciences Showa College Of Pharmaceutical Sciences
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Kuboki Yoshinori
Department Of Biochemistry Hokkaido University Dental School
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