Biochimica et Biophysica Acta (BBA) - Protein Structure
Steroid-protein interactions studied by fluorescence quenching
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Cited by (66)
Spectroscopic investigation of tolmetin interaction with human serum albumin
2013, Journal of Pharmaceutical and Biomedical AnalysisCitation Excerpt :Extrapolation of the linear portions of the experimental titration curve gave the stoichiometric point from which the mole ratio of bound tolmetin to HSA was obtained, but its value was not reported. The association constant was found to be 7.7 × 105 M−1 using an Eq. [7], which assumes the equivalence and independence of interaction sites in HSA. Due to the enormous popularity of using fluorescence quenching methodology to study ligand binding to HSA, the aim of this investigation is to use a correct data treatment, without extrapolations or using linearization methods, in order to obtain more accurate or at least more reliable results that describe the interaction between TOL and HSA.
Structural and ligand-binding properties of serum albumin species interacting with a biomembrane interface
2007, Journal of Pharmaceutical SciencesCitation Excerpt :The excitation wavelength of albumin was 295 nm, and fluorescence spectra were recorded at 300–370 nm. Drug‐binding parameters were calculated using the fluorescence quenching method.21 A fluorometric titration curve was constructed by plotting the tryptophanyl fluorescence intensity of albumin (Ex = 295 nm).
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1993, BBA - General Subjects
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Present address: Laboratory of Biophysical and Immunochemistry, Department of Chemistry, McGill University, Montreal, Quebec, Canada.