ABSTRACT
This chapter examines the physicochemical basis of protein retention in adsorption chromatography. The conventional approach to small-scale purification of biosolutes is predicated on the ability of chromatographic scientists to design and develop analytical systems that allow very high resolution. Attention to system residency and dwell effects, the nature of the heterogeneity of the distribution process and minimization of large changes in entropy due to the solute binding or permeability in the stationary-phase surfaces are all important parameters in this regard and find ample manifestation in preparative high-performance liquid chromatographic separations. The most successful separation techniques are those capable of probing the topography of the desired biopolymer in the feedstock mixture. Ion-exchange chromatography separations take advantage of the net charge and charge distribution of the surface of the biopolymer. The composite interplay between size-exclusion phenomena and solvophobic and coulombic interaction processes is a feature of all current chromatographic stationary phases.
