Pressure-jump relaxation studies of the association-dissociation reaction of e. coli ribosomes

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Abstract

The association-dissociation kinetics Of ribosomal particles from E. coli have been studied using a pressure-jump apparatus witn optical detection. Experiments on isolated subunits yield two relaxation times of about 10 and 700 ms, respectively. With mixtures of 30 S and 50 S particles an additional relaxation time of about 100 ms is observed, which is assigned to the equilibrium 30 S + 50 S ⇋ 70 S. The two other times are attributed to reversible equilibria between subunit monomers and subunit homo-associates.

References (17)

  • J.T. Penniston

    Arch. Biochem. Biophys.

    (1971)
  • W. Kauzmann

    Advan. Protein Chem.

    (1959)
  • R. Baierlein et al.
  • J.G. Hauge

    FEBS Lett.

    (1971)
  • A.D. Wolfe et al.

    FEBS Lett.

    (1973)
  • A. Wishnia et al.

    J. Mol Biol.

    (1975)
  • J.H. Cronenberger et al.

    J. Mol. Biol.

    (1975)
  • C. Guermant et al.

    Biophys. Chem.

    (1974)
There are more references available in the full text version of this article.

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