Studies on bacterial chemotaxis. IV. Interaction of maltose receptor with a membrane-bound chemosensing component.:IV. Interaction of Maltose Receptor with a Membrane-Bound Chemosensing Component

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  • KOIWAI Osamu
    Institute of Molecular Biology, Faculty of Science, Nagoya University
  • HAYASHI Hiroshi
    Institute of Molecular Biology, Faculty of Science, Nagoya University

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Description

Highly purified maltose receptor of Escherichia coli was bound to Sepharose 4B via a long spacer and affinity chromatography was performed to isolate the membrane-bound proteins having affinity for the maltose receptor. The experiments were carried out either in the pres-ence of maltose or in the absence of maltose and the proteins adsorbed on the matrix were identified by two-dimensional gel electrophoresis. The results showed that the maltose receptor interacted with the product of tar gene, one of the methyl-accepting chemotaxis proteins, only in the presence of maltose.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 86 (1), 27-34, 1979

    The Japanese Biochemical Society

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