Fluorimetric probes of the individual and competitive binding of 1-anilinonaphthalene-8-sulfonate, eosine and fluorescene to bovine serum albumin.
Fluorescence of 1-anilinonaphthalene-8-sulfonate (ANS) is greatly enhanced on its binding to bovine serum albumin (BSA). Fluorimetric titration shows that three ANS molecules bind per BSA molecule. The enhanced fluorescence of BSA-ANS is quenched by eosine (EOS); and one EOS physically displaces one ANS bound to BSA. The enhanced fluorescence of free ANS in the hydrophobic environment of the nonionic surfactant Triton X 100 is also quenched by EOS but by an energy transfer mechanism. The dye fluorescene (FLSN) also quenches the fluorescence of BSA-bound ANS, but by the energy transfer mechanism. The binding region of ANS in BSA has been speculated.
Pal
M K
MK
Department of Biochemistry & Biophysics, University of Kalyani, West Bengal, India.
Patra
S K
SK
D000817:Anilino Naphthalenesulfonates; D001667:Binding, Competitive; D004801:Eosine Yellowish-(YS); D005452:Fluoresceins; D005456:Fluorescent Dyes; D007700:Kinetics; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence / Q000379:methods
D000817:Anilino Naphthalenesulfonates; D005452:Fluoresceins; D005456:Fluorescent Dyes; D012710:Serum Albumin, Bovine; C027132:1-anilino-8-naphthalenesulfonate; D004801:Eosine Yellowish-(YS)