Biospecific interactions: their quantitative characterization and use for solute purification.
Biospecificity is due largely to the formation and dissociation of non-covalent complexes between small molecules and macromolecules, or between two macromolecules. The first part of this review is concerned with the use of such biospecificity in the fractionation and identification of solutes. Major emphasis is given to affinity chromatography, especially in regard to the practical considerations inherent in an experimental situation and to the wide range of specific interactions that can be utilized. The second part of the review considers the quantitative characterization of biospecific complex formation. The merits of frontal gel chromatography, electrophoretic methods and affinity chromatography are discussed, and special consideration is given to the effects of ligand and/or acceptor multivalency because of its relevance to many biospecific interactions. Finally attention is drawn to the feasibility of employing quantitative affinity chromatographic theory for the determination of association constants for antigen-antibody systems by radioimmunoassay and enzyme-linked immunosorbent assay techniques.
Winzor
D J
DJ
Department of Biochemistry, University of Queensland, St. Lucia, Australia.
De Jersey
J
J
D001671:Biochemistry / Q000379:methods*; D002846:Chromatography, Affinity / Q000379:methods*; D012995:Solubility; D012997:Solvents
D012997:Solvents