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Curve-fitting of Allosteric Binding Data

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Abstract

A RECENT theoretical investigation of the binding of a ligand to a polymerizing protein system1 extends the model of allosteric action based on isomerization2 to include reversible polymerization as a basis of these effects. We discuss here the possibility of defining uniquely an allosteric system from binding data in conjunction with other experimental evidence, and we consider results on the binding of succinate to aspartate transcarbamylase3 (EC 2.1.3.2) and of guanosinetriphosphate (GTP) to bovine liver glutamate dehydrogenase4 (EC 1.4.1.3).

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Authors and Affiliations

  1. Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria

    L. W. NICHOL & G. D. SMITH

  2. Department of Biochemistry, University of Queensland, St Lucia, Queensland

    D. J. WINZOR

Authors
  1. L. W. NICHOL
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  2. G. D. SMITH
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  3. D. J. WINZOR
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NICHOL, L., SMITH, G. & WINZOR, D. Curve-fitting of Allosteric Binding Data. Nature 222, 174–176 (1969). https://doi.org/10.1038/222174a0

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  • DOI: https://doi.org/10.1038/222174a0

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