[Study of the cholinesterase active site using a fluorescent probe].
We studied fluorescence of 9-amino-1,2,3,4-tetrahydroacridine hydrochloride (tacrine) in the presence of serum cholinesterase. Quenching of tacrine fluorescence dependent on cholinesterase activity has been revealed. A quenching mechanism is proposed; it includes formation of a complex and charge transfer mediated by excited tacrine molecule as well as indole of tryptophan residue from the periphery of cholinesterase active site.
Vetkin
D O
DO
Faculty of Physics, Moscow State University, Vorob'evy gory, Moscow, 119992 Russia.
Gaĭnullina
E T
ET
Karavaev
V A
VA
Nurmukhametov
R N
RN
Ryzhikov
S B
SB
Taranchenko
V F
VF
D000609:Aminoacridines / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002800:Cholinesterase Inhibitors / Q000378:metabolism*; D002802:Cholinesterases / Q000097:blood / Q000737:chemistry / Q000378:metabolism*; D005456:Fluorescent Dyes / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007211:Indoles / Q000737:chemistry / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013619:Tacrine / Q000378:metabolism*; D014364:Tryptophan / Q000737:chemistry
D000609:Aminoacridines; D002800:Cholinesterase Inhibitors; D005456:Fluorescent Dyes; D007211:Indoles; D013619:Tacrine; D014364:Tryptophan; D002802:Cholinesterases; C025902:acridine yellow