PURIFICATION AND CHARACTERIZATION OF TWO TYPES OF CYTISUS MULTIFLORUS HEMAGGLUTININ BY AFFINITY CHROMATOGRAPHY
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概要
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Two hemagglutinins were separated from extracts of Cytisus multiflorus seeds by successive affinity chromatographies on columns of galactose- and di-N-acetylchitobiose-Sepharose 4B. One was found to be inhibited by di-N-acetylchitobiose or tri-N-acetylchitotriose and shown to possess anti-H(O) activity [Cytisus-type anti-H(O) hemagglutinin designated as Cytisus multiflorus hemagglutinin I]. The other, which was not a blood group-specific hemagglutinin, was inhibited by galactose or lactose (hemagglutinin II). Hemagglutinins I and II were further purified by gel filtration on Sephacryl S-300. These Prepatations were homogeneous as judged by polyactylamide gel electrophoresis and gel filtration. The molecular weights of the purified hemagglutinins I and II were found to be 86000 by sedimentation equilibrium analysis and 80000 by gel filtration. On disc gel electrophoresis in the presence of sodium dodecyl sulfate and dithiothreitol, both hemagglutinins gave a single component of a molecular weight of 42000±2000,suggesting that these hemagglutinins are dimeric proteins of two identical subunits. Hemagglutinins I and II contain 2.7% and 1.5% carbohydrate, respectively, and only very small amounts of cystine and methionine were detected, but they are rich in aspartic acid and serine. Treatment of human O erythrocytes with a purified H-decomposing enzyme (α-L-fucosidase from Bacillus fulminans abolished the agglutinability of the cells with hemagglutinin I. This indicates that the L-fucosyl residue is important even for the H-specificity detected by this di-N-acetylchitobiose-specific hemagglutinin I.
- 公益社団法人日本薬学会の論文
著者
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Matsumoto Isamu
The Graduate School Of Humanities And Sciences Ochanomizu University
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YAMAMOTO Kazuo
Division of Cytokine Signaling, Department of Molecular Microbiology and Immunology, Nagasaki Univer
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MATSUMOTO Isamu
Department of Obstetrics and Gynecology, Faculty of Medicine, Kagoshima University
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YAMAMOTO KAZUMITSU
Research and Development Division, Dainippon Pharmaceutical Co., Ltd.
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Yamamoto K
Proteolysis Research Laboratory Graduate School Of Pharmaceutical Sciences Kyushu University
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Matsumoto Isamu
Department Of Chemistry Faculty Of Science Ochanomizu University
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Tsuji T
Microbiology Faculty Of Pharmaceutical Sciences Hoshi University
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Tsuji Tsutomu
Division Of Chemical Toxicology And Immunochemistry Faculty Of Pharmaceutical Sciences University Of
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OSAWA TOSHIAKI
Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University
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Osawa Toshiaki
Division Of Chemical Toxicology And Immunochemistry Faculty Of Pharmaceutical Sciences University Of
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Osawa Toshiaki
Laboratory Of Molecular Medicine Department Of Integrated Biosciences Graduate School Of Frontier Sc
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Konami Yukiko
Laboratory Of Molecular Medicine Department Of Integrated Biosciences Graduate School Of Frontier Sc
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KONAMI YUKIKO
Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University
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OSAWA Toshiaki
Yakult Central Institute for Microbiological Research
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Osawa Toshiaki
Division Of Chemical Toxicology And Immunochemistry Faculty Of Pharmaceutical Science University Of
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Yamamoto Kazuo
Division Of Cytokine Signaling Department Of Molecular Microbiology And Immunology Nagasaki Universi
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Yamamoto Kazuo
Laboratory Of Molecular Medicine Department Of Integrated Biosciences Graduate School Of Frontier Sc
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Matsumoto Isamu
Department of Chemistry, Faculty of Science, Ochanomizu University
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MATSUMOTO ISAMU
Department of Biochemistry, Kurume University School of Medicine
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