AI Article Synopsis
- Experiments on bovine serum albumin (BSA) using potentiometric titration and electrophoretic light scattering reveal how specific ions bind to the protein's surface, particularly at a physiological concentration of 0.1 M.
- Anion binding occurs at acidic pH, where the protein is positively charged, and also at the isoionic point, following a Hofmeister series ranking different anions in order of binding strength.
- The study highlights the complexity of measuring these effects and suggests that different sodium salts can influence the surface charge of BSA, aligned with the Hofmeister series.
Article Abstract
Experiments on bovine serum albumin (BSA) via potentiometric titration (PT) and electrophoretic light scattering (ELS) are used to study specific-ion binding. The effect is appreciable at a physiological concentration of 0.1 M. We found that anions bind to the protein surface at an acidic pH, where the protein carries a positive charge (Z(p) > 0), according to a Hofmeister series (Cl(-) < Br(-) < NO(3)(-) < I(-) < SCN(-)), as well as at the isoionic point (Z(p) = 0). The results obtained require critical interpretation. The measurements performed depend on electrostatic theories that ignore the very specific effects they are supposed to reveal. Notwithstanding this difficulty, we can still infer that different 1:1 sodium salts affect the BSA surface charge/pH curve because anions bind to the BSA surface with an efficiency which follows a Hofmeister series.
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