[Interaction between strychnine and bovine serum albumin].
OBJECTIVE
To study the interaction between strychnine and bovine serum albumin.


METHODS
Fluorescence spectroscopy and ultraviolet spectroscopy were used.


RESULTS
The 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.


CONCLUSIONS
The interaction between strychnine and BSA was driven mainly by hydrophobic force.
Zhao
Jin
J
College of Food Science and Technology, University of Hebei, Baoding 071000, China.
Wang
Zhi
Z
Wu
Qiu-hua
QH
Yang
Xiu-min
XM
Wang
Chun
C
Hu
Yan-xue
YX
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004735:Energy Transfer; D010946:Plants, Medicinal / Q000737:chemistry; D011485:Protein Binding; D012639:Seeds / Q000737:chemistry; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013331:Strychnine / Q000737:chemistry* / Q000378:metabolism; D031461:Strychnos nux-vomica / Q000737:chemistry; D013816:Thermodynamics
D012710:Serum Albumin, Bovine; D013331:Strychnine