TY - JOUR
T1 - 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
AU - Fujii, Yuki
AU - Kawsar, Sarkar M.A.
AU - Matsumoto, Ryo
AU - Yasumitsu, Hidetaro
AU - Ishizaki, Naoto
AU - Dogasaki, Chikaku
AU - Hosono, Masahiro
AU - Nitta, Kazuo
AU - Hamako, Jiharu
AU - Taei, Matsui
AU - Ozeki, Yasuhiro
N1 - Funding Information:
This work was supported in part by a Grant-In-Aid for scientific research (no. 1021009100 to YO and SMAK) from the Japan Society for the Promotion of Science , Japanese Association for Marine Biology (JAMBIO, no. 22-02 to YO and HY) and Strategic Research Project from Yokohama City University (no. G2201 to YO and HY). The authors are thankful to Dr. Robert A. Kanaly for his critical reading of this manuscript.
PY - 2011/1
Y1 - 2011/1
N2 - 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.
AB - 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.
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U2 - 10.1016/j.cbpb.2010.09.002
DO - 10.1016/j.cbpb.2010.09.002
M3 - Article
C2 - 20837158
AN - SCOPUS:78649635168
SN - 1096-4959
VL - 158
SP - 30
EP - 37
JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
IS - 1
ER -