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- W1977211541 abstract "The relationship between the lone tryptophan residue at position 214 and drug binding sites (Sites I and II) in human serum albumin (HSA) was studied by fluorescence energy transfer. The distance between the lone tryptophan residue and ligands bound to HSA was estimated by Förster's equation, taking into consideration the degree of ligand binding at these sites, as determined from binding parameters (binding constant, k, and the number of binding sites, n). For all ligands investigated, the distance in each case appeared to asymptotically decrease when the occupation ratio of the binding sites increased with ligand concentration. When the primary binding site of each ligand in HSA was almost saturated, the distance attained a constant value, making possible a somewhat more exact determination of the distance. The distance ranged from ∼22 to 23 Å for ligands typical of Site I (warfarin, dansylamide, dansylglutamine), and ∼16.1 to 17.5 Å for ligands typical of Site II (dansylsarcosine, dansylproline, dansylglycine, diazepam, flufenamic acid)." @default.
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- W1977211541 date "1987-05-01" @default.
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- W1977211541 title "Fluorescence Energy Transfer Study of the Relationship Between the Lone Tryptophan Residue and Drug Binding Sites in Human Serum Albumin" @default.
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- W1977211541 doi "https://doi.org/10.1002/jps.2600760510" @default.
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