Purification and Properties of a Lectin from the Fruitbodies(Biological Chemistry)
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概要
- 論文の詳細を見る
A lectin was purified to homogeneity from the fruitbodies of Flammulina velutipes by conventional purification procedures. The purified lectin was demonstrated to be a dimeric protein consisting of two identical subunits with an apparent molecular mass of 11 kDa. The lectin was an acidic protein with a pi value of 5.4, and devoid of cysteine, methionine, and histidine as amino acid constituents. Its hemagglutinating activity was totally unaffected by mono- and oligosaccharides and glycosides, but inhibited by some desialylated glycoproteins. Immunological assays revealed that no protein cross-reacting with rabbit anti-F. velutipes lectin antibody was apparently present in vegetatively growing mycelia but was distributed throughout the fruitbody at different concentrations.
- 1988-06-23
著者
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Nakata Munehiro
Department Of Bilchemistry Faculty Of Science Saitama University
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TSUMURAYA Yoichi
Department of Biochemistry and Molecular Biology, Faculty of Science, Saitama University
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Hashimoto Yohichi
Department of Biochemistry, Faculty of Science, Saitama University
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Tsumuraya Yoichi
Department Of Bilchemistry Faculty Of Science Saitama University
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Tsumuraya Y
Saitama Univ. Saitama Jpn
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Yatohgo Takemi
Department Of Bilchemistry Faculty Of Science Saitama University
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Hashimoto Y
Central Research Institute Tsukuba R&d Center Fuji Oil Co. Ltd.
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YAMAMOTO Shigeru
Laboratory of Serology and Biochemistry, National Research Institute of Police Science
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Nakata Munehiro
Department Of Applied Biochemistry Tokai University School Of Engineering
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Yamamoto Shigeru
Laboratory Of Serology And Biochemistry National Research Institute Of Police Science
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