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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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Sodium Dodecyl Sulfate

2001
[151-21-3] C12H25NaO4S (MW 288.38) InChI = 1S/C12H26O4S.Na/c1-2-3-4-5-6-7-8-9-10-11-12-16-17(13,14)15;/h2-12H2,1H3,(H,13,14,15);/q;+1/p-1 InChIKey = DBMJMQXJHONAFJ-UHFFFAOYSA-M (used in surfactant-based reaction media) Alternate Names: SDS; sodium lauryl sulfate; SLS.
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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.
L O, Narhi, M, Zukowski, T, Arakawa
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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
Rita, de Cássia Comis Wagner   +1 more
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Gas chromatographic determination of sodium dodecyl sulfate

Analytical Biochemistry, 1974
Abstract A gas chromatographic method has been developed for the determination of sodium dodecyl sulfate. The method is sensitive, reasonably accurate, and uninfluenced by the presence of protein. The method depends upon the formation of 1-dodecanol and inorganic sulfate by acidic hydrolysis of sodium dodecyl sulfate (4 n HCl, 2 hr, 100°C).
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Removal of sodium dodecyl sulfate from proteins

Analytical Biochemistry, 1978
Effective removal of sodium dodecyl sulfate from proteins in water or sodium phosphate buffer was achieved by column chromatography using the ion-retardation resin AG11A8. An average recovery of 83% protein was obtained, while 0.1 to 1.4 moles of sodium dodecyl sulfate remained on each mole of protein.
O H, Kapp, S N, Vinogradov
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Micelles in Mixtures of Sodium Dodecyl Sulfate and a Bolaform Surfactant

Langmuir, 2006
Mixtures composed of water, sodium dodecyl sulfate (SDS), and a bolaform surfactant with two aza-crown ethers as polar headgroups (termed Bola C-16) were investigated by modulating the mole ratios between the components. The two surfactants have ionic and nonionic, but ionizable, headgroups, respectively.
Rita Muzzalupo   +6 more
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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 ...
William J Knox, Terence O Parshall
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Fate and Effects of the Surfactant Sodium Dodecyl Sulfate

1993
Sodium dodecyl sulfate is the most widely used of the anionic alkyl sulfate surfactants. Its surface-active properties make it important in hundreds of household and industrial cleaners, personal care products, and cosmetics. It is also used in several types of industrial manufacturing processes, as a delivery aid in pharmaceuticals, and in biochemical
M M, Singer, R S, Tjeerdema
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The Mechanism of Hemolysis of Erythrocytes by Sodium Dodecyl Sulfate

Annals of the New York Academy of Sciences, 2005
Abstract: The results of a study of vesicular‐hemolytic action of anionic detergent sodium dodecyl sulfate on human erythrocytes are presented. Possible molecular events underlying detergent‐induced pore formation in the erythrocyte membrane are discussed.
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