Enthalpy of antibody--cytochrome c binding.

@article{Raman1995EnthalpyOA,
  title={Enthalpy of antibody--cytochrome c binding.},
  author={C. S. Raman and Mark J Allen and Barry T Nall},
  journal={Biochemistry},
  year={1995},
  volume={34 17},
  pages={5831-8}
}
High-sensitivity titration calorimetry is used to measure changes in enthalpy, heat capacity, and protonation for binding of two monoclonal antibodies (MAbs) to topologically distinct surfaces of cytochrome c. MAb 2B5 binds near the exposed heme crevice in a reaction involving proton uptake, while there is no change in protonation for MAb 5F8 binding to the opposite side of the molecule. Both antibodies have association rate constants with the activation enthalpy and viscosity dependence… CONTINUE READING