A d-galactose-binding lectin purified from coronate moon turban, Turbo (Lunella) coreensis, with a unique amino acid sequence and the ability to recognize lacto-series glycosphingolipids

Yuki Fujii, Sarkar M.A. Kawsar, Ryo Matsumoto, Hidetaro Yasumitsu, Naoto Ishizaki, Chikaku Dogasaki, Masahiro Hosono, Kazuo Nitta, Jiharu Hamako, Matsui Taei, Yasuhiro Ozeki

研究成果: Article査読

13 被引用数 (Scopus)

抄録

A divalent, cation-independent d-galactose-binding lectin was purified from coronate moon turban Turbo (Lunella) coreensis. This lectin recognizes d-galactose and is a 38-kDa dimeric protein consisting disulphide-bonded 22-kDa polypeptides under non-reducing and reducing conditions of sodium dodecyl sulphate-polyacrylamide gel electrophoresis, respectively. Haemagglutination activity was inhibited by d-galactose, N-acetyl d-galactosamine, melibiose, lactose, porcine stomach mucin, asialofetuin and bovine submaxillary mucin. The lectin has tolerance for pH 5-11 and temperature until 50 °C for 1. h. The lectin strongly aggregated Gram-negative bacteria, such as Vibrio parahaemolyticus and Salmonella O7, but weakly Gram-positive strain as Staphylococcus aureus and Bacillus subtilis. The glycan-binding profile of this lectin was evaluated using frontal affinity chromatography technology and the lectin appeared to recognize oligosaccharides such as lacto-series glycosphingolipids contained in blood type A and H substances in addition to complex-type N-linked glycoproteins. Partial primary structures of 139 amino acid residues of this lectin were determined from N-terminus polypeptides and 8 peptides derived by cleavage with lysyl-endopeptidase. The primary structure was slightly similar to other known sequences of lectin; however, a repeating motif has been included.

本文言語English
ページ(範囲)30-37
ページ数8
ジャーナルComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
158
1
DOI
出版ステータスPublished - 01-2011

All Science Journal Classification (ASJC) codes

  • 生化学
  • 生理学
  • 分子生物学

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