A simpler analysis for the measurement of second virial coefficients by self-interaction chromatography.
We describe a thermodynamic approach that supports the adoption of a simplified procedure for the determination of protein second virial coefficients (B(2)) 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 B(2). 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.
Winzor
Donald J
DJ
Department of Biochemistry, School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Qld 4072, Australia. d.winzor@uq.edu.au
Scott
David J
DJ
Wills
Peter R
PR
D002845:Chromatography / Q000379:methods*; D003460:Crystallization; D006863:Hydrogen-Ion Concentration; D008027:Light; D015233:Models, Statistical; D009113:Muramidase / Q000737:chemistry; D012542:Scattering, Radiation; D013816:Thermodynamics
D009113:Muramidase