caa a22 4500 397555164 CHVBK 20180308164759.0 cr unu---uuuuu 161202e199602 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021249 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021249 Synthetic Glycogels for Affinity Electrophoresis: A Facile and Efficient Method for Investigating Sugar-Lectin Interaction [Elektronische Daten] [Masashi Ohmae, Sayuri Suzuki, Seiichi Tokura, Norio Nishi, Shin-Ichiro Nishimurat] A novel and efficient method for analyzing sugar-lectin interaction using affinity electrophoresis (AEP) is described. Polyacrylamide gels covalently conjugated with 2-acetamido-2-deoxy-D-glucopyranose (GlcNAc) residues were successfully prepared by radical copolymerization of highly reactive 3-(N-acryloylamino)propyl 2-acetamido-2-deoxy-β-D-glucopyranoside with acrylamide in the presence of N,N'-methylenebi8acrylamide (BIS). When the glycogels carrying various densities of GlcNAc branches were employed for polyacrylamide gel electrophoresis (PAGE) of lectins, the mobilities of wheat germ agglutinin (WGA) were specifically reduced by increasing the concentrations of the GlcNAc residues in gels, although concanavalin A (Con A) showed no significant change in the mobility. It was also demonstrated that the association constant of WGA with immobilized GlcNAc residue can be determined by combined use of this stable glycogel and an automated gel-scanning system associated with fluorometric spectroscopy. The association constant of WGA with the GlcNAc moiety was estimated to be 1.24×104 M−1 © by the Journal of Biochemistry Regular Papers nationallicence affinity electrophoresis nationallicence fluorometric detection nationallicence glycogel nationallicence glycomonomer nationallicence lectin-sugar interaction nationallicence Ohmae Masashi Division of Bio-Science, Graduate School of Environmental Earth Science, Hokkaido University, Kita-ku, Sapporo 060 aut Suzuki Sayuri Division of Biological Sciences, Graduate School of Science, Hokkaido University, Kita-ku, Sapporo 060 aut Tokura Seiichi Division of Bio-Science, Graduate School of Environmental Earth Science, Hokkaido University, Kita-ku, Sapporo 060 aut Nishi Norio Division of Bio-Science, Graduate School of Environmental Earth Science, Hokkaido University, Kita-ku, Sapporo 060 aut Nishimurat Shin-Ichiro Division of Biological Sciences, Graduate School of Science, Hokkaido University, Kita-ku, Sapporo 060 aut The Journal of Biochemistry Oxford University Press 119/2(1996-02), 367-371 0021-924X 119:2<367 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021249 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021249 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ohmae Masashi Division of Bio-Science, Graduate School of Environmental Earth Science, Hokkaido University, Kita-ku, Sapporo 060 aut NATIONALLICENCE 700 1- Suzuki Sayuri Division of Biological Sciences, Graduate School of Science, Hokkaido University, Kita-ku, Sapporo 060 aut NATIONALLICENCE 700 1- Tokura Seiichi Division of Bio-Science, Graduate School of Environmental Earth Science, Hokkaido University, Kita-ku, Sapporo 060 aut NATIONALLICENCE 700 1- Nishi Norio Division of Bio-Science, Graduate School of Environmental Earth Science, Hokkaido University, Kita-ku, Sapporo 060 aut NATIONALLICENCE 700 1- Nishimurat Shin-Ichiro Division of Biological Sciences, Graduate School of Science, Hokkaido University, Kita-ku, Sapporo 060 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/2(1996-02), 367-371 0021-924X 119:2<367 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford