title: Isolation and biochemical characterization of Apios tuber lectin.
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 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.
authors.affiliation: Graduate School of Life Sciences, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai 980-8577, Japan. eri.kenmochi@gmail.com.
authors.forename: Eri
authors.initials: E
authors.lastname: Kenmochi
authors.affiliation: Graduate School of Life Sciences, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai 980-8577, Japan. rashelkabir@ru.ac.bd.
authors.forename: Syed Rashel
authors.initials: SR
authors.lastname: Kabir
authors.affiliation: Graduate School of Life Sciences, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai 980-8577, Japan. ogawa@biochem.tohoku.ac.jp.
authors.forename: Tomohisa
authors.initials: T
authors.lastname: Ogawa
authors.affiliation: Department of Biochemistry and Microbiology, Nelson Mandela Metropolitan University, Port Elizabeth 6031, South Africa. ryno.naude@nmmu.ac.za.
authors.forename: Ryno
authors.initials: R
authors.lastname: Naude
authors.affiliation: National Institute of Advanced Industrial Science and Technology, 1-1-1 Umezono, Ibaraki 305-8568, Japan. h-tateno@aist.go.jp.
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Tateno
authors.affiliation: National Institute of Advanced Industrial Science and Technology, 1-1-1 Umezono, Ibaraki 305-8568, Japan. jun-hirabayashi@aist.go.jp.
authors.forename: Jun
authors.initials: J
authors.lastname: Hirabayashi
authors.affiliation: Graduate School of Life Sciences, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai 980-8577, Japan. muramoto@biochem.tohoku.ac.jp.
authors.forename: Koji
authors.initials: K
authors.lastname: Muramoto
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D018938:Caco-2 Cells; D002241:Carbohydrates / Q000032:analysis; D017097:Electric Impedance; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000737:chemistry*; D006384:Hemagglutination / Q000187:drug effects; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007477:Ions; D008670:Metals / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010455:Peptides / Q000737:chemistry; D037121:Plant Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D035281:Plant Tubers / Q000737:chemistry*; D011817:Rabbits; D017386:Sequence Homology, Amino Acid; D013025:Glycine max / Q000737:chemistry; D013696:Temperature
chemical_list: D002241:Carbohydrates; D007477:Ions; D008670:Metals; D010455:Peptides; D037121:Plant Lectins