Purification, Characterization, and cDNA Cloning of a Novel Lectin from the Green Alga, Codium barbatum
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概要
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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.
- 2012-04-23
著者
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Hori Kanji
Food Science And Biofunctions Division Graduate School Of Biosphere Science Hiroshima University
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Hirayama Makoto
Food Science And Biofunctions Division Graduate School Of Biosphere Science Hiroshima University
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PRASEPTIANGGA Danar
Food Science and Biofunctions Division, Graduate School of Biosphere Science, Hiroshima University