Interactions of two amphiphilic penicillins with myoglobin in aqueous buffered solutions: a thermodynamic and spectroscopy study.

@article{Taboada2004InteractionsOT,
  title={Interactions of two amphiphilic penicillins with myoglobin in aqueous buffered solutions: a thermodynamic and spectroscopy study.},
  author={Pablo Taboada and Yolanda Blanco Fern{\'a}ndez and V. Becerra Mosquera},
  journal={Biomacromolecules},
  year={2004},
  volume={5 6},
  pages={2201-11}
}
The interactions and complexation process of the amphiphilic penicillins sodium cloxacillin and sodium dicloxacillin with horse myoglobin in aqueous buffered solutions of pH 4.5 and 7.4 have been examined by equilibrium dialysis, zeta-potential, isothermal titration calorimetry (ITC) and UV-Vis absorbance techniques. A more opened structure of the protein molecules is detected as a consequence of the reduction of pH from 7.4 to 4.5. Binding isotherms and derived Hill coefficients reflect a… CONTINUE READING