Purification, Characterization, and cDNA Cloning of a Novel Lectin from the Green Alga, Codium barbatum

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A novel lectin (CBA) was isolated from the green alga, <I>Codium barbatum</I>, by conventional chromatographic methods. The hemagglutination-inhibition profile with sugars and glycoproteins indicated that CBA had preferential affinity for complex type <I>N</I>-glycans but not for monosaccharides, unlike the other known <I>Codium</I> lectins specific for <I>N</I>-acetylgalactosamine. CBA consisted of an SS-linked homodimer of a 9257-Da polypeptide containing seven cysteine residues, all of which were involved in disulfide linkages. The cDNA of the CBA subunit coded a polypeptide (105 amino acids) including the signal peptide of 17 residues. The calculated molecular mass from the deduced sequence was 9705 Da, implying that the four C-terminal amino acids of the CBA proprotein subunit were post-translationally truncated to afford the mature subunit (84 amino acids). No significantly similar sequences were found during an <I>in silico</I> search, indicating CBA to be a novel protein. CBA is the first <I>Codium</I> lectin whose primary structure has been elucidated.

収録刊行物

  • Bioscience, biotechnology, and biochemistry

    Bioscience, biotechnology, and biochemistry 76(4), 805-811, 2012-04-23

    公益社団法人 日本農芸化学会

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各種コード

  • NII論文ID(NAID)
    10030752017
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09168451
  • NDL 記事登録ID
    023593184
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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