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- W1989898391 abstract "The binding of 2-p-toluidinylnaphthalene-6-sulfonate to L-isoleucyl-tRNA synthetase is associated with a strong increase of fluorescence intensity and a concomitant shift in the wavelength of maximum emission. Binding of the fluorophore does not interfere with substrate binding nor the ATP-32PPi exchange activity of the enzyme. The formation of binary and ternary enzymesubstrate complexes is indicated by a significant quenching of the fluorescence. Dissociation constants were determined from the degree of quenching as a function of the substrate concentration. Evaluation of spectrofluorometric data suggest that substrate binding is associated with a conformation change in which tryptophan side chains of the protein are involved." @default.
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- W1989898391 date "1971-10-01" @default.
- W1989898391 modified "2023-10-12" @default.
- W1989898391 title "2-p-toluidinylnaphthalene-6-sulfonate, a fluorescent reporter group for L-isoleucyl-tRNA synthetase" @default.
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- W1989898391 doi "https://doi.org/10.1016/0006-291x(71)90834-5" @default.
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