The dissociation of glucose oxidase by sodium n-dodecyl sulphate

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The dissociation of glucose oxidase by sodium n-dodecyl sulphate.

1. The enzymic activity of glucose oxidase was determined as a function of pH and sodium n-dodecyl sulphate (SDS) concentration. 2. Glucose oxidase is not deactivated by SDS at pH 6 even after prolonged incubation, but is deactivated at pH 4.3 and 3.65. 3. Sedimentation-rate analysis showed that glucose oxidase dissociates into its two subunits at pH 5 and below, and sedimentation-equilibrium e...

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Thermal Analysis of Adenosine Deaminase in the Presence of Sodium N-Dodecyl Sulphate

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FOLDING 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...

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THERMODYNAMIC STUDIES OF THE INTERACTION OF SODIUM N-DODECYL, SULPHATE WITH CALF - THYMUS WISTONE H3

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...

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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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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1982

ISSN: 0264-6021

DOI: 10.1042/bj2030285