title: [Interaction between strychnine and bovine serum albumin].
abstract: 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.
authors.affiliation: College of Food Science and Technology, University of Hebei, Baoding 071000, China.
authors.forename: Jin
authors.initials: J
authors.lastname: Zhao
authors.forename: Zhi
authors.initials: Z
authors.lastname: Wang
authors.forename: Qiu-hua
authors.initials: QH
authors.lastname: Wu
authors.forename: Xiu-min
authors.initials: XM
authors.lastname: Yang
authors.forename: Chun
authors.initials: C
authors.lastname: Wang
authors.forename: Yan-xue
authors.initials: YX
authors.lastname: Hu
mesh_terms: 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
chemical_list: D012710:Serum Albumin, Bovine; D013331:Strychnine