## Abstract The interaction of caffeine with bovine serum albumin (BSA) under physiological condition was investigated by fluorescence, UVโvis absorption and circular dichroism (CD) spectroscopy. Fluorescence data revealed that the fluorescence quenching of BSA by caffeine was a result of the forma
Fluorometric determination of drug-protein association constants: Binding of pamaquine by bovine serum albumin
โ Scribed by Datta V. Naik; W. Larry Paul; Stephen G. Schulman
- Publisher
- John Wiley and Sons
- Year
- 1975
- Tongue
- English
- Weight
- 371 KB
- Volume
- 64
- Category
- Article
- ISSN
- 0022-3549
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The usefulness of bovine serum albumin (BSA) as a model protein for testing NMR methods for the study of protein-ligand interactions is discussed. Isothermal titration calorimetry established the binding affinity and stoichiometry of the specific binding site for L-tryptophan, D-tryptophan, naproxen