[Interaction between warfarin and bovine serum albumin detected by spectrometry].
The interaction between warfarin and bovine serum albumin (BSA) under pseudophysiological conditions was investigated by UV-Vis absorption spectrometry and spectrofluorimetry. The quenching mechanism of BSA by warfarin was discussed. It showed that the quenching process was a dynamic quenching, and the quenching constants were 6.05 x 10(4) L x mol(-1) at 16 degrees C and 6. 14 x 10(4) L x mol(-1) at 37 degrees C, separately. Based on the Förster theory of non-radiative energy transfer, the energy transfer efficiency and the distance of BSA to warfarin were calculated, which was 0.37 and 3.15 nm, respectively.
Yan
Yang
Y
First Affiliated Hosptical, Medical School of Xi' an Jiaotong University, Xi' an 710061, China.
Pei
Ruo-hui
RH
Yan
Hong-tao
HT
D004735:Energy Transfer; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013056:Spectrophotometry, Ultraviolet / Q000379:methods*; D013816:Thermodynamics; D014859:Warfarin / Q000737:chemistry*
D012710:Serum Albumin, Bovine; D014859:Warfarin