Publication | Closed Access
Properties of the Interface Between Two Immiscible Electrolytes in the Presence of Proteins
43
Citations
0
References
1984
Year
ElectrolytesEngineeringElectrode-electrolyte InterfaceCs+ TransferAdsorbed ProteinsProtein Phase SeparationChemistryInterface Between TwoBiosensing SystemsProtein FoldingBioanalysisAnalytical ChemistryElectrochemical InterfaceBiophysicsInterfacial ProcessInitial Bsa AdsorptionBiochemistryBiopolymersImmiscible ElectrolytesElectrochemistryProtein EngineeringElectroanalytical SensorMedicineElectrochemical Surface Science
The influence of adsorbed proteins on electrochemical properties of the nitrobenzene‐aqueous interface has been investigated using cyclic voltammetric and impedance techniques. Upon addition of 4 μg/ml ovalbumin cyclic voltammetric values for Cs+ transfer shifted from nearly temperature independent reversible values to more temperature‐dependent irreversible values. These effects were especially pronounced at lower temperatures and suggested formation of a surface film. The cyclic voltammetry of a wide range of concentrations of bovine serum albumin (BSA) in base L/L electrolytes was also studied. Interfacial ac impedance measurements indicated an increase in diffuse layer capacitance accompanied initial BSA adsorption. At high protein concentrations, an adsorbed phase was formed which facilitates faradaic transfer of ions across an otherwise blocked interface.