By use of a accurately thermostated disc gel electrophoresis apparatus, apparent dissociation constants of various biospecific interactions at varying temperatures were calculated. From the van't Hoff plots, thermodynamic constants were calculated. The obtained values well coincided with those values which were obtained by other techniques, such as equilibrium dialysis or fluorescence quenching and enhancement technique.
Affinity of hydrophilic interactions such as those between concanavalin A and dextran or glycogen phosphorylase and glycogen, decreases with a rise in temperature of the reaction medium. In these interactions, standard enthalpy change, Δ
H°, and standard entropy change, Δ
S°, were calculated as negative one. On the contrary, affinity of hydrophobic interaction, such as those between aromatic hapten and anti-aromatic hapten antibody increases with a rise in temperature. In these interactions, Δ
H° and Δ
S° were calculated as positive one.
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