Interaction between warfarin and bovine serum albumin detected by spectrometry / 药学学报
Acta Pharmaceutica Sinica
; (12): 1224-1227, 2008.
Article
in Zh
| WPRIM
| ID: wpr-232613
Responsible library:
WPRO
ABSTRACT
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.
Full text:
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Index:
WPRIM
Main subject:
Protein Binding
/
Spectrometry, Fluorescence
/
Spectrophotometry, Ultraviolet
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Thermodynamics
/
Warfarin
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Serum Albumin, Bovine
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Chemistry
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Energy Transfer
/
Methods
Language:
Zh
Journal:
Acta Pharmaceutica Sinica
Year:
2008
Type:
Article