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Sodium dodecyl sulfate (SDS) or sodium lauryl sulfate (SLS), sometimes written sodium laurilsulfate, is an organic compound with the formula CH 3 (CH 2) 11 OSO 3 Na and structure H 3 C−(CH 2) 11 −O−S(=O) 2 −O − Na +. It is an anionic surfactant used in many cleaning and hygiene products. This compound is the sodium salt of the 12 ...
[16] [17] Fendler et al. measured the partitioning of 14 radiolabeled amino acids using sodium dodecyl sulfate (SDS) micelles. Also, amino acid side chain affinity for water was measured using vapor phases. [14] Vapor phases represent the simplest non polar phases, because it has no interaction with the solute. [18]
Sodium dodecyl sulfate (SDS), a common detergent, may be found in protein extracts because it is used to lyse cells by disrupting the membrane lipid bilayer and to denature proteins for SDS-PAGE. While other detergents interfere with the assay at high concentration, the interference caused by SDS is of two different modes, and each occurs at a ...
Sodium octyl sulfate: 0.13: anionic surfactant Sodium dodecyl sulfate: 0.0083: anionic surfactant Sodium tetradecyl sulfate: 0.0021: anionic surfactant Decyltrimethylammonium bromide: 0.065: cationic surfactant Dodecyltrimethylammonium bromide: 0.016: cationic surfactant Hexadecyltrimethylammonium bromide: 0.00092: cationic surfactant Penta ...
In colloidal chemistry, the critical micelle concentration (CMC) of a surfactant is one of the parameters in the Gibbs free energy of micellization. The concentration at which the monomeric surfactants self-assemble into thermodynamically stable aggregates is the CMC.
Proteins of the erythrocyte membrane separated by SDS-PAGE according to their molecular masses. SDS-PAGE (sodium dodecyl sulfate–polyacrylamide gel electrophoresis) is a discontinuous electrophoretic system developed by Ulrich K. Laemmli which is commonly used as a method to separate proteins with molecular masses between 5 and 250 kDa.
Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) is a method of separating molecules based on the difference of their molecular weight. At the pH at which gel electrophoresis is carried out the SDS molecules are negatively charged and bind to proteins in a set ratio, approximately one molecule of SDS for every 2 amino acids.
A detergent such as sodium dodecyl sulfate (SDS) can be used to dissolve cell membranes and keep membrane proteins in solution during purification; however, because SDS causes denaturation, milder detergents such as Triton X-100 or CHAPS can be used to retain the protein's native conformation during complete purification.