Abstract
We describe a thermodynamic approach that supports the adoption of a simplified procedure for the determination of protein second virial coefficients (B2) by self-interaction chromatography. Its major advantage over the original method is a decrease in the number of parameters to which magnitudes must be assigned for the determination of B2. Improved correlation of virial coefficients obtained by the chromatographic procedure with those obtained by light scattering is achieved by taking into account the twofold larger magnitudes of the former because of the experimental distinction between free and immobilized protein molecules in self-interaction chromatography.
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