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 (Zp > 0), according to a Hofmeister series (Cl- < Br- < NO3 - < I- < SCN-), as well as at the isoionic point (Zp = 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

Hofmeister Challenges: Ion Binding and Charge of the BSA Protein as Explicit Examples

MEDDA, LUCA;CUGIA, FRANCESCA;MONDUZZI, MAURA;SALIS, ANDREA
2012

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 (Zp > 0), according to a Hofmeister series (Cl- < Br- < NO3 - < I- < SCN-), as well as at the isoionic point (Zp = 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
INTERFACIAL WATER-STRUCTURE; BOVINE SERUM-ALBUMIN; ENZYMATIC-ACTIVITY; PH MEASUREMENTS; SERIES; ANION; SALT; LYSOZYME; ELECTROLYTE; SPECIFICITY
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11584/98196
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