The interaction between β-lactoglobulin and sodium N-dodecyl sulphate
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The Unexpected Effect of Sodium Arsenate on the Interaction between Histone H1 and Sodium N-Dodecyl Sulphate
A Study was made on the interaction between histon H1 and sodium n-dodecyl sulphate (SDS) in the presence of sodium arsenate inside a phosphate buffer of pH 6.4, using spectroscopy and equilibrium dialysis at 27 °C. The binding data has been used to obtain the gibbs free energy in terms of a theoretical model based on the Wyman binding potential. The binding data hs been analysed...
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The binding of Sodium n-dodecyl sulphate (SDS) to histone H3 was studied in the pH range 3.2-10 by equilibrium dialysis at 27? and 3 7 ?c .T he binding data have been used to obtain the Gibbs free energy of interaction using a theoretical model of the Wyman binding potential; and the enthalpy of interaction from the temperature dependence of theequilibriumconstantsfronr theVan't Hoff re1ati...
متن کاملFOLDING OF THE INTERACTION OF HISTONE HI WITH SODIUM N-DODECYL SULPHATE
The effects of sodium n-dodecyl sulphate (SDS) on the structure of histone HI has been studied by a combination of e:quilibrium dialysis, U.V. spectroscopy ; polyacrylamide gel electrophoresis, protein titration and viscometery techniques using, 2.5 mM phosphate buffer, pH 6.4. The interaction of H, and SDS in contrast tomanyothel-protein-SDS interactions is organized between V 40 to 70. A...
متن کاملInteraction Studies of Sodium N-Dodecyl Sulphate and Protons to Nistone H1
The relationship between the binding of sodium n-dodecyl sulphate and protons to histone H1 has been investigated by equilibrium dialysis and titrimetry. The data cover the pH range 3.2-10 and surfactant concentrations up to 3.0×10-3 mol dm-3. A theoretical approach based on the binding potential concept of Wyman is presented and has been used to make estima...
متن کاملthe unexpected effect of sodium arsenate on the interaction between histone h1 and sodium n-dodecyl sulphate
a study was made on the interaction between histon h1 and sodium n-dodecyl sulphate (sds) in the presence of sodium arsenate inside a phosphate buffer of ph 6.4, using spectroscopy and equilibrium dialysis at 27 °c. the binding data has been used to obtain the gibbs free energy in terms of a theoretical model based on the wyman binding potential. the binding data hs been analysed in terms of hi...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1976
ISSN: 0264-6021
DOI: 10.1042/bj1530713