Isolation and Characterization of a D-Galactose-binding Lectin from the Acorn Barnacle Balanus rostratus

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  • Toda Michitoshi
    Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University
  • Jimbo Mitsuru
    Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University
  • Muramoto Koji
    Graduate School of Agriculture, Department of Biological Resource Sciences, Tohoku University
  • Sakai Rvuichi
    Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University
  • Kamiya Hisao
    Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University

書誌事項

タイトル別名
  • Isolation and Characterization of a D-Galactose-binding Lectin from the Acorn Barnacle <i>Balanus rostratus</i>
  • Isolation and Characterization of a D G

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The hemolymph of the acorn barnacle Balanus rostratus showed hemagglutinating activity and inhibition of calcium carbonate crystallization. A lectin having D-galactose-binding specificity was isolated from the hemolymph by a combination of affinity chromatography on acid-treated agarose gel and HPLC. The purified lectin was dependent on the presence of calcium ion for hemagglutinating activity. In SDS-PAGE, it gave one protein band (25kDa) under a reduced condition, while it gave two components (35 and 95kDa) without a reducing agent. The molecular mass of the intact lectin was estimated to be 120kDa by HPLC on TSK G-3000SW. Isolectric point was determined to be pH 4.4. The same amino-terminal sequence, Tyr-Val-Ser-Asn-Gln-Ser-Val-Glu-Pro-Asp-Ser-Ala-Asp-Thr-Ala, was obtained with the purified lectin as well as the components observed in SDS-PAGE. The purified lectin did not inhibit calcium carbonate crystallization at 1mg/30ml, although the hemolymph inhibited the crystallization at 0.1mg protein/30ml. The inhibitory factor(s) was an acidic and small molecular-weight compound(s).

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