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• W2164558174 abstract "Steady-state and dynamic fluorescence titrations show that: (a) the complex between β-lactoglobulin (BLG) and 1-anilinonaphthalene-8-sulfonate (ANS) displays a heterogeneous equilibrium with large changes in the binding strength vs. pH and ion concentration; and (b) the fluorescence response of bound ANS reveals two separate lifetimes that suggest two different sites (or binding modes). While steady-state fluorescence titrations yield effective values of the binding constant and of the bound ANS quantum efficiency, it is shown that, by combining steady-state fluorescence and lifetime decay of ANS, it is possible to give quantitative estimates of the association constants for each site. When heading from the acid (pH∼2) to the native state (pH∼6) the main result is a very large reduction of the effective binding constant. This and the results of titrations vs. ionic strength suggest that electrostatic interactions are a major contribution to ANS binding to BLG." @default.
• W2164558174 created "2016-06-24" @default.
• W2164558174 creator A5032541175 @default.
• W2164558174 creator A5036385479 @default.
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• W2164558174 date "1999-07-01" @default.
• W2164558174 modified "2023-09-29" @default.
• W2164558174 title "Evidence of heterogeneous 1-anilinonaphthalene-8-sulfonate binding to β-lactoglobulin from fluorescence spectroscopy" @default.
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• W2164558174 doi "https://doi.org/10.1016/s0167-4838(99)00105-3" @default.
• W2164558174 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10407141" @default.
• W2164558174 hasPublicationYear "1999" @default.
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