Quantitative considerations of the consequences of an interplay between ligand binding and reversible adsorption of a macromolecular solute |
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Authors: | DJ Winzor LD Ward LW Nichol |
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Institution: | Department of Biochemistry, University of Queensland, St. Lucia, Queensland 4067, Australia;Department of Physical Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra, A.C.T. 2601, Australia |
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Abstract: | Explicit expressions are derived which determine the equilibrium composition of mixtures comprising a multivalent, insoluble matrix, a multivalent, macromolecular solute (acceptor) and a univalent ligand. With three-reactant mixtures of this type a range of combinations of interactions is possible wherein the ligand interacts with either the acceptor or the matrix, in either event perturbing the acceptor-matrix equilibria. Theory encompassing this range of possibilities is written in terms of a single site-binding constant for each type of interaction to account, in general terms, for both multiple binding and crosslinking effects. These explicit thermodynamic relationships are discussed, with the use of reported findings on several biological systems, in two frameworks. First, it is established that the theory is applicable to the quantitative interpretation of affinity chromatography experiments designed to elucidate the thermodynamic interaction parameters governing the various types of interacting system. Second, it is emphasized that the relationships are also relevant to metabolite-induced changes in the subcellular distribution of macromolecular species. |
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Keywords: | Address for Correspondence: Professor L W Nichol Department of Physical Biochemistry John Curtin School of Medical Research Australian National University P O Box 334 Canberra City A C T 2601 Australia |
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