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Keywords = American groundnut

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16 pages, 1674 KiB  
Article
Isolation and Biochemical Characterization of Apios Tuber Lectin
by Eri Kenmochi, Syed Rashel Kabir, Tomohisa Ogawa, Ryno Naude, Hiroaki Tateno, Jun Hirabayashi and Koji Muramoto
Molecules 2015, 20(1), 987-1002; https://doi.org/10.3390/molecules20010987 - 9 Jan 2015
Cited by 24 | Viewed by 7720
Abstract
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Lectins)
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