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Molecules 2015, 20(1), 987-1002;

Isolation and Biochemical Characterization of Apios Tuber Lectin

Graduate School of Life Sciences, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai 980-8577, Japan
Department of Biochemistry and Molecular Biology, University of Rajsahi, Rajshahi 6205, Bangladesh
Department of Biochemistry and Microbiology, Nelson Mandela Metropolitan University, Port Elizabeth 6031, South Africa
National Institute of Advanced Industrial Science and Technology, 1-1-1 Umezono, Ibaraki 305-8568, Japan
Author to whom correspondence should be addressed.
Academic Editors: Tzi Bun NG, Jack Ho WONG and Evandro Fei FANG
Received: 30 November 2014 / Accepted: 5 January 2015 / Published: 9 January 2015
(This article belongs to the Special Issue Lectins)
Full-Text   |   PDF [1674 KB, uploaded 9 January 2015]   |  


Apios tuber lectin, named ATL, was isolated from Apios americana Medikus by two chromatography steps, hydrophobic chromatography and anion-exchange chromatography. The minimum concentration required for the hemagglutination activity toward rabbit erythrocytes of ATL was 4 μg/mL. ATL was composed of a homodimer of 28.4 kDa subunits. The amino acid sequence of ATL was similar to those of other legume lectins. The lectin showed moderate stability toward heating and acidic pH, and the binding affinity against several monosaccharides, such as D-glucosamine and D-galactosamine. ATL also bound to desialylated or agalactosylated glycoproteins such as asialo and agalacto transferrin. ATL decreased the transepithelial electrical resistance across human intestinal Caco-2 cell monolayers, suggesting the effect on the tight junction-mediated paracellular transport. View Full-Text
Keywords: Apios americana; lectin; American groundnut; legume lectin Apios americana; lectin; American groundnut; legume lectin

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Kenmochi, E.; Kabir, S.R.; Ogawa, T.; Naude, R.; Tateno, H.; Hirabayashi, J.; Muramoto, K. Isolation and Biochemical Characterization of Apios Tuber Lectin. Molecules 2015, 20, 987-1002.

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