The l-arabinose permease system in Escherichia coli B/r

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Abstract

The l-arabinose permease system of Escherichia coli B/r was characterized by measuring l-[i-14C]arabinose uptake by an l-arabinose isomerase-less mutant. This organism accumulates l-arabinose via an inducible, energy-dependent system that exhibits the kinetic properties of permease-mediated transport. The system consists of at least 2 parts: an entrance reaction that obeys Michealis-Menten kinetics and an exit reaction with a high temperature coefficient that exhibits first-order kinetics. Inhibition studies indicate that the system may also mediate the transport of d-xylose, d-frucose, and d-galactose. A “cold shock” phenomenon which results in a rapid loss in accumulated carbohydrates is described.

References (20)

  • A. Kepes

    Biochim. Biophys. Acta

    (1960)
  • B.L. Horecker et al.

    J. Biol. Chem.

    (1960)
  • B.L. Horecker et al.

    J. Biol. Chem.

    (1960)
  • M.J. Osborn et al.

    J. Biol. Chem.

    (1961)
  • P. Hoffee et al.

    Biochim. Biophys. Acta

    (1964)
  • H.T. Hagihira et al.

    Biochim. Biophys. Acta

    (1963)
  • J. Gross et al.

    Virology

    (1959)
  • O.H. Lowry et al.

    J. Biol. Chem.

    (1951)
  • A. Koch

    Biochim. Biophys. Acta

    (1964)
  • A. Kepes et al.
There are more references available in the full text version of this article.

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Present address: Department of Biological Sciences, University of California, Santa Barbara, Calif., U.S.A.

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