Analysis of glucose-protein interaction using <i>p</i>-hydroxyacetophenone-Sepharose affinity resin &mdash;Glucose decreases alcohol dehydrogenase activity <i>in vitro</i>&mdash;

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  • Negoro Munetaka
    Department of Chemical and Biological Engineering, Ube National College of Technology
  • Sawano Mina
    Department of Chemical and Biological Engineering, Ube National College of Technology
  • Sawamura Hiromi
    Department of Dietary Environment Analysis, School of Human Science and Environment, Himeji Institute of Technology, University of Hyogo
  • Ebara Shuhei
    Department of Dietary Environment Analysis, School of Human Science and Environment, Himeji Institute of Technology, University of Hyogo
  • Watanabe Toshiaki
    Department of Dietary Environment Analysis, School of Human Science and Environment, Himeji Institute of Technology, University of Hyogo

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  • Analysis of glucose-protein interaction using <i>p</i>-hydroxyacetophenone-Sepharose affinity resin —Glucose decreases alcohol dehydrogenase activity <i>in vitro</i>—

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The purpose of the present study was to find the possibility of a glucose-protein interaction using p-hydroxyacetophenone (p-HAP)-Sepharose resin. Additionally, two proteins were identified as p-HAP-Sepharose binding proteins. In this study, seven polypeptides were found to have an affinity with p-HAP in the liver cytosolic fraction. More specifically, this study demonstrated that the four polypeptides from the seven also have an affinity with glucose. Moreover, to confirm the results from this experiment using a p-HAP affinity column, a commercially available horse liver alcohol dehydrogenase (HLADH) was examined. HLADH bounded to a p-HAP affinity column was eluted by both glucose and p-HAP. The in vitro enzymatic activity of the HLADH, in the presence of ethanol as a substrate, was significantly decreased by incubation with glucose (up to 250 mM). These results suggested that glucose has an affinity with HLADH and decreases its activity in vitro.<br>

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