Results 251 to 260 of about 146,598 (282)
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Interaction between casein and sodium dodecyl sulfate

Journal of Colloid and Interface Science, 2007
The interaction of the anionic surfactant sodium dodecyl sulfate (SDS) with 2.0 mg/ml casein was first investigated using isothermal titration calorimetry (ITC), dynamic light scattering (DLS), and fluorescence spectra. ITC results show that individual SDS molecules first bind to casein micelles by the hydrophobic interaction.
Yan Liu, Rong Guo
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Removal of sodium dodecyl sulfate from proteins

Analytical Biochemistry, 1975
Abstract A convenient and relatively simple electrodialysis method for the removal of sodium dodecyl sulfate (SDS) from proteins is described. Six samples can be processed simultaneously. The kinetics of removal of SDS from proteins by equilibrium dialysis and electrodialysis have been studied.
Leonard Warren, George P. Tuszynski
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The interaction of sodium dodecyl sulfate with gelatin

Journal of Colloid and Interface Science, 1970
Abstract The interaction of sodium dodecyl sulfate with gelatin at pH 7 has been investigated by measuring the surface tension of aqueous SDS/gelatin mixtures. Comparison of the resulting data with comparable precipitation data obtained at pH 4.1 indicates that the compositions of the complexes formed above and below the isoelectric point are quite ...
Terence O Parshall, William J Knox
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Molecular Mobility in Solid Sodium Dodecyl Sulfate

The Journal of Physical Chemistry B, 2011
Here we report on the molecular mobility in solid sodium dodecyl sulfate (SDS), a commonly used surfactant, as measured by high-resolution neutron scattering in the temperature range 175-400 K. While the quasielastic data showed the presence of dynamical motion at and above 210 K, the fixed energy window (FEW) data indicated that the dynamics is ...
S. Mitra   +4 more
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Stability of aprA-subtilisin in sodium dodecyl sulfate

Archives of Biochemistry and Biophysics, 1988
The effect of sodium dodecyl sulfate (SDS) on the structure and activity of aprA-subtilisin, a secreted bacterial serine protease which is 85% homologous to subtilisin BPN', was examined. The addition of SDS resulted in the slow conversion of the subtilisin from the intact protein to the completely unfolded form of the enzyme.
Linda O. Narhi   +2 more
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Sodium dodecyl sulfate in protein chemistry

Biosystems, 1975
This review summarizes in a brief manner the main aspects of the application of sodium dodecyl sulfate (SDS) to protein chemistry. The principal problems of SDS-polyacrylamide gel electrophoresis are described, as well as the anomalous behavior of protein-SDS complexes and the inactivation of enzymes due to variable binding of SDS to the polypeptides ...
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Hair protein removal by sodium dodecyl sulfate

Colloids and Surfaces B: Biointerfaces, 2005
The effect of sodium dodecyl sulfate (SDS) on protein loss was studied. Three kinds of human hair were tested by rubbing or immersion in water or immersion in SDS solution, at 25, 40 and 70 degrees C. Under friction, hair treated with SDS solution loses seven times more protein than in water, while by immersion, protein loss is roughly two times higher
Inés Joekes   +1 more
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Micellization of sodium dodecyl sulfate and polyoxyethylene dodecyl ethers in solution [PDF]

open access: possibleColloid and Polymer Science, 2009
The effect of polyoxyethylene type nonionic surfactants (C12E n n = 3, 4, 5, 6, 7 and 8) on the aqueous solution of sodium dodecyl sulfate (SDS) in absence and presence of NaCl was examined using small-angle neutron scattering (SANS), dynamic light scattering (DLS), and viscosity measurements ...
Pratap Bahadur   +3 more
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Thermal degradation of sodium dodecyl sulfate

Journal of Agricultural and Food Chemistry, 1984
Certaines fractions produites lors de la degradation thermique du sodium dodecyl sulfate possedent une cytotoxicite superieure a celle de l'aniline. Dans le cas du tabac, ces residus resultant de l'utilisation agricole peuvent etre soumis a de hautes temperatures lors de son utilisation chez les ...
Zbigniew Kortylewicz   +2 more
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Relationship between micellar lifetime and foamability of sodium dodecyl sulfate and sodium dodecyl sulfate/1-hexanol mixtures [PDF]

open access: possibleLangmuir, 1991
The interface between air and surfactant solution expands rapidly during the foam generation process. Surfactant molecules in the solution should adsorb onto the newly created surface to stabilize foam. As surfactant monomers adsorb on the surface, micelles disintegrate to provide additional monomers to adsorb on the expanding interface of foam.
Seong Geun Oh, Dinesh O. Shah
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