Influence of hydrogen and chloride ions on the interaction between sulfaethidole and bovine serum albumin studied by microcalorimetric and acid-base titrimetric methods.

@article{Janssen1979InfluenceOH,
  title={Influence of hydrogen and chloride ions on the interaction between sulfaethidole and bovine serum albumin studied by microcalorimetric and acid-base titrimetric methods.},
  author={Lambert H. M. Janssen and T H Nelen},
  journal={The Journal of biological chemistry},
  year={1979},
  volume={254 12},
  pages={5300-3}
}
From earlier studies it is known that bovine serum albumin has one high affinity binding site and several lower affinity sites for the sulfa drug N1-(5-ethyl-1,3,4-thiadiazol-2-yl)sulfanilamide (sulfaethidole) (Kostenbauder, H.B., Jawad, M.J., Perrin, J.H., and Averhart, V. (1971) J. Pharm. Sci. 60, 1658-1660). This binding has been further studied using… CONTINUE READING