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

PRASEPTIANGGA, Danar and HIRAYAMA, Makoto and HORI, Kanji (2012) Purification, Characterization, and cDNA Cloning of a Novel Lectin from the Green Alga, Codium barbatum. Biosci. Biotechnol. Biochem, 76 (4). pp. 805-811.

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    Abstract

    A novel lectin (CBA) was isolated from the green alga, Codium barbatum, by conventional chromato- graphic methods. The hemagglutination-inhibition pro- file with sugars and glycoproteins indicated that CBA had preferential affinity for complex type N-glycans but not for monosaccharides, unlike the other known Codium lectins specific for N-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 calcu- lated molecular mass from the deduced sequence was 9705Da, 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 in silico search, indicating CBA to be a novel protein. CBA is the first Codium lectin whose primary structure has been elucidated.

    Item Type: Article
    Subjects: Q Science > Q Science (General)
    Q Science > QH Natural history > QH301 Biology
    Divisions: Lembaga Penelitian dan Pengabdian Kepada Masyarakat - LPPM
    Depositing User: Anis Fagustina
    Date Deposited: 09 May 2014 16:13
    Last Modified: 09 May 2014 16:13
    URI: https://eprints.uns.ac.id/id/eprint/15516

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