Thermodynamics of the interaction of epsilon-dinitrophenyl-L-lysine and the subunits (Fab) of bovine colostral immunoglobulin G1 anti-dinitrophenyl antibody.
Investigation of the binding of epsilon-DNP-1-lysine to the subunits (Fab') of bovine colostral IgG1 anti-DNP over a wide range of temperatures yielded non-linear van't Hoff plots with curvatures which were indicative of large positive heat capacity changes. Thermodynamic functions which were calculated using a non-linear least-squares procedure revealed an enthalpy-entropy compensation mechanism for binding. While the enthalpy factor was the driving force for the hapten-subunit interaction(s) at low temperatures, the entropy factor assumed greater importance with increasing temperatures. In addition, the enthalpy-entropy compensation plot for the interaction of epsilon-DNP-1-lysine with bovine colostral Fab' anti-DNP, intact anti-DNP IgG1 and rabbit IgG anti-DNP revealed a constant compensation temperature (T degrees c) of 27 degrees which might be considered as indicative of a single kind of protein-solvent conformation.
D000818:Animals; D000937:Antigen-Antibody Reactions; D002417:Cattle; D003126:Colostrum / Q000276:immunology; D004136:Dinitrobenzenes / Q000276:immunology*; D005260:Female; D006241:Haptens; D007140:Immunoglobulin Fab Fragments; D009578:Nitrobenzenes / Q000276:immunology*; D013696:Temperature; D013816:Thermodynamics
D004136:Dinitrobenzenes; D006241:Haptens; D007140:Immunoglobulin Fab Fragments; D009578:Nitrobenzenes