Purification and Characterization of the Lectins of the soft Coral <i>Lobophytum variatum</i>

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  • Goto-Nance Rina
    Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University
  • Muramoto Koji
    Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University Faculty of Agriculture, Tohoku University
  • Zenpo Yohko
    Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University
  • Kamiya Hisao
    Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University

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  • Purification and Characterization of the Lectins of the Soft Coral Lobophytum variatum
  • Purification and Characterization of th

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Abstract

The extract of the soft coral Lobophytum variatum agglutinated horse erythrocytes but not human ABO or rabbit erythrocytes in the presense of calcium ions. The activity was inhibited by mucin Type I from the bovine submaxillary gland and also by simple sugars such as D-ribose and N-acetylneuraminic acid. Two lectins, LVL-1 and LVL-2, were purified by gel filtration on Sepharose 4 B succeeded by ionexchange chromatography on Mono-Q. Both lectins were glycoproteins composed of covalently bonded subunits of 53 kDa. The sequence of the amino-terminal region of LVL-1 was determined as Ala-Ile-Asn-Gln-Ser-Ser-Gly-Asn-Leu-(X)-Asp-Arg-Leu-Gln-Glu-Arg-Phe-(X)-Leu-Asp-His-, where X is anunidentified residue.

Journal

  • Fisheries science

    Fisheries science 62 (2), 297-301, 1996

    The Japanese Society of Fisheries Science

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