Temperature dependency of thermodynamic parameters in interactions between hen egg-white lysozyme (HEL) and anti-HEL antibodies.
We examined temperature dependency of thermodynamic parameters in the interactions between hen egg-white lysozyme (HEL) and anti-HEL antibody, D1.3, and two mutant antibodies. The DeltaH degrees values appeared to decrease biphasically in the temperature range from 10 to 45 degrees C with the apparent inflection point around 30 degrees C. The DeltaG degrees calculated from the KA values showed only small differences because of entropy and enthalpy compensation. It has been argued that large negative values of heat capacity change (DeltaCp degrees), if observed, are mainly derived from hydrophobic interactions. However, the observed DeltaCp degrees values were too high to be ascribed only to hydrophobic interactions. Moreover, addition of methanol did not cause a decrease in the absolute value of DeltaCp degrees.
Yasui
H
H
Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi 470-1192, Japan.
Ito
W
W
Kurosawa
Y
Y
D019943:Amino Acid Substitution; D000818:Animals; D000936:Antigen-Antibody Complex / Q000737:chemistry* / Q000276:immunology; D002645:Chickens; D004529:Egg White; D007128:Immunoglobulin Fragments / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D007143:Immunoglobulin Heavy Chains / Q000235:genetics / Q000276:immunology; D007135:Immunoglobulin Variable Region / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D000432:Methanol; D009113:Muramidase / Q000737:chemistry* / Q000276:immunology; D009154:Mutation; D012996:Solutions; D013696:Temperature; D013816:Thermodynamics
D000936:Antigen-Antibody Complex; D007128:Immunoglobulin Fragments; D007143:Immunoglobulin Heavy Chains; D007135:Immunoglobulin Variable Region; D012996:Solutions; C055966:immunoglobulin Fv; D009113:Muramidase; D000432:Methanol