Preparation and Characterization of Functional Domains of Porcine Plasma Fibronectin
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概要
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The relations between surface hydrophobicities and binding properties of the functional domains of porcine plasma fibronectin were investigated. Porcine and human plasma fibronectins were adsorbed on a hydrophobic column with butyl or phenyl ligands in the presence of 0.5M ammonium sulfate, and recovered in a single peak by decreasing the concentration of ammonium sulfate to 0M, indicating that both fibronectins have very high surface hydrophobicities. Limited proteolysis of porcine plasma fibronectin with thermolysin yielded five fragments, of 140-150kDa, 43kDa, 25kDa, 17kDa and 14kDa. Analysis of the digests by high performance hydrophobic interaction chromatography and affinity chromatography on heparinor gelatin-Sepharose, together with previous results, indicated that the 140-150kDa fragment has cell-attachment and heparin-binding domains, the 43kDa fragment a collagen-binding domain, the 25kDa fragment a heparin-binding domain, the 17kDa fragment a fibrin-binding domain and the 14kDa fragment a heparin-binding domain. The three heparin-binding fragments were found to have a wide range of surface hydrophobicities, of which the 140-150kDa fragment had the lowest, the 25kDa fragment higher, and the 14kDa fragment the highest among all the fragments. The 43kDa and 17kDa fragments had surface hydrophobicities as high as that of fibronectin. Carbohydrate analysis and lectin binding studies using horseradish peroxidase conjugated lectins showed that porcine plasma fibronectin has 10 biantennary N-linked carbohydrate chains on the 43kDa and 140-150kDa fragments. It is noteworthy that the 43kDa collagenbinding fragment contributes to the high surface hydrophobicity of intact fibronectin in spite of the high content of carbohydrates (60% of the total carbohydrates).
- お茶の水女子大学の論文
著者
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Matsumoto I
お茶の水女子大学
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Matsumoto Isamu
The Graduate School Of Humanities And Sciences Ochanomizu University
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MATSUMOTO Isamu
Department of Obstetrics and Gynecology, Faculty of Medicine, Kagoshima University
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HAYASHI MASAO
Department of Biology, Ochanomizu University
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Hayashi Masao
Department Of Biology Ochanomizu University
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Seno N
Department Of Chemistry Ochanomizu University
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Seno Nobuko
Department Of Chemistry Faculty Of Science Ochanomizu University
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Ogawa Haruko
Department Of Chemistry Faculty Of Science Ochanomizu University
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Kitagaki-ogawa Haruko
Department Of Chemistry Ochanomizu University
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Ogawa Haruko
Department Of Advanced Biosciences Graduate School Of Humanities And Sciences Ochanomizu University
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Matsumoto I
Ochanomizu Univ. Tokyo
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Matsumoto Isamu
Matsumoto Institute Of Life Science
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Matsumoto Isamu
Division Of Human Genetics Medical Research Institute Kanazawa Medical University
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Matsumoto Isamu
Department Of Chemistry Faculty Of Science Ochanomizu University
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Matsumoto Isamu
Graduate School Of Humanities And Sciences Ochanomizu University
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Hayashi-Nagai Atsuko
Department of Chemistry Faculty of Science, Ochanomizu University
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Hayashi-nagai Atsuko
Department Of Chemistry Faculty Of Science Ochanomizu University
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Hayashi Masao
Department Of Astronomy Graduate School Of Science The University Of Tokyo
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MATSUMOTO ISAMU
Department of Biochemistry, Kurume University School of Medicine
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