Theory of counterion electrophoresis. Guidelines for determination of ligand-binding parameters |
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Authors: | J R Cann N H Fink |
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Institution: | Department of Biochemistry/Biophysics/Genetics, University of Colorado Health Sciences Center, 4200 E. 9th Avenue, Denver, CO 80262, U.S.A. |
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Abstract: | A theory is formulated to provide guidelines for the quantitative interpretation of steady-state counterion electrophoretic patterns (T.-H. Ueng and F. Bronne, Arch. Biochem. Biophys. 197 (1979) 205) in terms of intrinsic ligand-binding constant and number of binding sites on the protein molecule. Briefly, the prescribed procedure calls for extrapolation of the steady-state binding constant to infinite dilution of protein to obtain a quantity which is the product of a readily evaluated kinetic factor and the intrinsic binding constant. On the other hand, extrapolation of the steady-state number of binding sites to infinite dilution can probably be dispensed with if determined at a reasonably low protein concentration. |
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Keywords: | Counterion electrophoresis Counterion electrophoresis theory Ligand binding parameter determination Steady-state binding parameter Thermodynamic binding parameter |
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