ENTHALPY-ENTROPY COMPENSATION IN DINITROPHENYL-ANTI-DINITROPHENYL ANTIBODY INTERACTION(S)

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  • 1 January 1977
    • journal article
    • research article
    • Vol. 32  (2) , 111-119
Abstract
The effect of varying the temperature over a wide range (-3.degree. C to 67.degree. C) on the binding of .epsilon.-DNP[dinitrophenol]-L-lysine to bovine colostral anti-DNP IgG1 [immunoglobulin G1], and also rabbit anti-DNP IgG revealed non-linear van''t Hoff plots. The extent of the curvatures were 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 ethalpy-entropy compensation mechanism for hapten-antibody binding. The enthalpy factor was the primary contributor for the binding process at low temperatures, but at increasing temperatures the entropy factor assumed greater importance. At physiological temperature (37.degree. C), the entropy factor was the major contributor to the free energy reaction for rabbit anti-DNP IgG, while for bovine colostral anti-DNP IgG1 it was predominant at temperatures higher than 37.degree. C.