1. Subunit molecular weights of 76000-82000 were obtained for native and alkylated Tamm-Horsfall glycoprotein by gel filtration on Sephadex G-200 in the presence of sodium dodecyl sulphate. 2. A further estimate of the subunit molecular weight of 79 000± 4000 was obtainedby disc gel electrophoresis in sodium dodecyl sulphate. 3. A minimum value of the chemical molecular weight of 79000±6000 was...

The thermal denaturation of adenosine deaminase (ADA) has been investigated in the presence of sodium n-dodecyl sulphate (SDS) over the temperature range of (293-363K) in 2.5 mM phosphate buffer, pH 6.4 by temperature scanning spectroscopy. The interaction of SDS caused the folding of adenosine deaminanse resulting in a decrease of TH (temperature of minimum solubility), TS<...

The binding of sodium n-dodecyl sulphate (SDS) to Aspergillus niger catalase in various ionic strengths at pH 6.4 and a temperature of 27? and 37?C has been studied over a range of SDS concentrations using equilibrium dialysis and fluorescence spectroscopy techniques. The binding data were used and interpreted in terms of theoretical models (Scatchard Equation and Wyman Binding Potential). ...

The interaction of sodium n-dodecyl sulphate (SDS) with histones in phosphate buffer pH 6.4 has been studied spectroscopically and by equilibrium dialysis. The enthalpies of interaction and the spectroscopic data suggest different structural stability for histones-SDS interaction. The linear relation between enthaly and absorbtion was determined by the equation of m= , where m is the sta...

Dehydroepiandrosterone sulphate is one of the most important neurosteroids. In the present paper, we studied the effect of dehydroepiandrosterone sulphate on persistent sodium currents and its mechanism and functional consequence with whole-cell patch clamp recording method combined with a pharmacological approach in the rat medial prefrontal cortex slices. The results showed that dehydroepiand...

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...

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...