Enthalpy-entropy compensation in dinitrophenyl--anti-dinitrophenyl antibody interaction(s).
The effect of varying the temperature over a wide range (-3 dergees -67 degrees) on the binding of xi-DNP-L-Lysine to bovine colostral anti-DNA IgG1, and also rabbit anti-DNP IgG revealed non-linear van't Hoff plots. The extent of the curvatures were found to be indicative of large positive heat capacity changes; and the thermodynamic parameters, calculated using a non-linear least-squares computer procedure for these anti-DNP antibody preparations, revealed an enthalpy-entropy compensation mechanism for hapten-antibody binding. The enthalpy factor was found to be the primary contributor for the binding process at low temperatures, but at increasing temperatures the entropy factor assumed greater importance. At physiological temperature (37 degrees), the entropy factor was the major contributor to the free energy of reaction for rabbit anti-DNP IgG, while for bovine colostral anti-DNP IgG it was predominant at temperatures higher than 37 degrees.
D000818:Animals; D000937:Antigen-Antibody Reactions; D001666:Binding Sites, Antibody; D002417:Cattle; D003126:Colostrum / Q000276:immunology; D004136:Dinitrobenzenes / Q000276:immunology*; D006241:Haptens; D007074:Immunoglobulin G; D009578:Nitrobenzenes / Q000276:immunology*; D011817:Rabbits; D013696:Temperature; D013816:Thermodynamics
D004136:Dinitrobenzenes; D006241:Haptens; D007074:Immunoglobulin G; D009578:Nitrobenzenes