Purification and Properties of a Lectin from the Fruitbodies of Flammulina velutipes |
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| Authors: | Takemi Yatohgo Munehiro Nakata Yoichi Tsumuraya Yohichi Hashimoto Shigeru Yamamoto |
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| Institution: | 1. Department of Biochemistry, Faculty of Science, Saitama University, 255 Shimo-ohkubo, Urawa, Saitama 338, Japan;2. Laboratory of Serology and Biochemistry, National Research Institute of Police Science, 6 Sanbun-cho, Chiyoda-ku, Tokyo 102, Japan |
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| Abstract: | 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-i7. velutipes lectin antibody was apparently present in vegetatively growing mycelia but was distributed throughout the fruitbody at different concentrations. |
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| Keywords: | lactosucrose calcium absorption bone rat |
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