Interaction between strychnine and bovine serum albumin.
- Author:
Jin ZHAO
1
;
Zhi WANG
;
Qiu-hua WU
;
Xiu-min YANG
;
Chun WANG
;
Yan-xue HU
Author Information
- Publication Type:Journal Article
- MeSH: Animals; Binding Sites; Cattle; Energy Transfer; Plants, Medicinal; chemistry; Protein Binding; Seeds; chemistry; Serum Albumin, Bovine; chemistry; metabolism; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Strychnine; chemistry; metabolism; Strychnos nux-vomica; chemistry; Thermodynamics
- From: Acta Pharmaceutica Sinica 2006;41(7):666-670
- CountryChina
- Language:Chinese
-
Abstract:
AIMTo study the interaction between strychnine and bovine serum albumin.
METHODSFluorescence spectroscopy and ultraviolet spectroscopy were used.
RESULTSThe static quenching and the non-radiation energy transfer are the two main reasons to leading the fluorescence quenching of BSA. The apparent combining constants (K(A)) between strychnine and BSA are 3.72 x 10(3) at 27 degrees C, 4.27 x 10(3) at 37 degrees C, 4.47 x 10(3) at 47 degrees C and the combining sites are 1.01 +/- 0.03. The combining distance (r = 3.795 nm) and energy transfer efficiency (E = 0.0338) are obtained by Förster's non-radiation energy transfer mechanism.
CONCLUSIONThe interaction between strychnine and BSA was driven mainly by hydrophobic force.
