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  • Title: Thermodynamics of the interaction of epsilon-dinitrophenyl-L-lysine and the subunits (Fab) of bovine colostral immunoglobulin G1 anti-dinitrophenyl antibody.
    Author: Szewczuk MR, Mukkur TK.
    Journal: Immunology; 1977 Jul; 33(1):11-6. PubMed ID: 873571.
    Abstract:
    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.
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