Influence of the N-B transition of human serum albumin on the structure of the warfarin-binding site.

@article{KasaiMorita1987InfluenceOT,
  title={Influence of the N-B transition of human serum albumin on the structure of the warfarin-binding site.},
  author={S Kasai-Morita and Toshiharu Horie and Shoji Awazu},
  journal={Biochimica et biophysica acta},
  year={1987},
  volume={915 2},
  pages={277-83}
}
The fluorescence quantum yield of warfarin increased with the viscosity of the medium and showed good correlation with it. The internal rotation of the acetonylbenzyl group of a warfarin molecule may thus possibly decrease in a viscous medium. the fluorescence quantum yield of warfarin bound to human serum albumin increased with the pH of the medium in the pH range of 6.2-9.0. Fluorescence-emission maximum wavelengths of warfarin bound to human serum albumin indicated a small blue-shift with… CONTINUE READING