Dodecyl sulfate, Na-salt

Na-dodecyl sulfate (SDS) belongs to the most powerful solubilizers for integral membrane proteins.

SDS has the advantage of avoiding aggregation but mostly it causes denaturation of the membrane proteins. Some of the SDS-solubilized membrane proteins which are in a denatured state, e.g. a 5´-nucleotidase or a neuraminidase, have been successfully renatured.

Na-dodecyl sulfate is a potent fibrinolytic surfactant.

SDS is of  importance in the isolation of DNA without phenol extraction. It has also proved to be of value for the separation of virus proteins and double-stranded RNAs; an SDS-KCl precipitation allows a quick and selective separation by a single step.

Several protein assays may be improved by modification with Na-dodecyl sulfate.

Na-dodecyl sulfate is used preferently in polyacrylamide gel electrophoresis for the separation of proteins and peptides and is often applied to optimize chromatographic separations.

Synonyms: SDS, sodium lauryl sulfate

CAS registry number: [151-21-3]

Molecular formula: C12H25O4S . Na

Relative molecular mass (Mr): 288.4

Classification: Anionic surfactant

Literature specifications:
•    Critical micellar concentration (CMC): 8.1 mM
•    Aggregation number (Na): 60 - 62
•    Krafft point (TK): 9 °C
•    Hydrophilic-lipophilic balance (HLB): 40


Bibliography

Characterization and Determination of Enzymes

Adney, W.S., Rivard, C.J., Grohmann, K. a. Himmel, M.E. (1989) Detection of extracellular hydrolytic enzymes in the anaerobic digestion of municipal solid waste. Biotechnol. Appl. Biochem. 11, 387-400.

Eder, K., Reichlmayr-Lais, A.M. a. Kirchgessner, M. (1989) Calcium-magnesium-ATPase determination in red blood cell membranes with use of sodium dodecyl sulfate. Trace Elem. Med. 6, 64-9.

Eder, K., Reichlmayr-Lais, A.M. a. Kirchgessner, M. (1989) Studies on the determination of sodium-potassium-ATPase in red blood cell membranes. J. Trace Elem. Electrolytes Health Dis. 3, 151-9.

Henderson, L.M., Chappell, J.B. a. Jones, O. T.G. (1989) Superoxide generation is inhibited by phospholipase A2 inhibitors. Role for phospholipase A2 in the activation of the NADPH oxidase. Biochem. J. 264, 249-55.

Ishida, K., Takeshige, K., Takasugi, S. a. Minakami, S. (1989) GTP-dependent and -in-dependent activation of superoxide producing NADPH oxidase in a neutrophil cell-free system. FEBS Lett. 243, 169-72.

Sha'ag, D. (1989) Sodium dodecyl sulfate dependent NADPH-oxidation: an alternative method for assaying NADPH-oxidase in a cell-free system. J. Biochem. Biophys. Methods 19, 121-8.

Shpungin, S., Dotan, I., Abo, A. a. Pick, E. (1989) Activation of the superoxide forming NADPH-oxidase in a cell-free system by sodium dode-cyl sulfate. Absolute lipid dependence of the solubilized enzyme. J. Biol. Chem. 264, 9195-203.

Tanaka, K., Yoshimura, T. a. Ichihara, A. (1989) Role of substrate in reversible activation of proteasomes (multi-protease complexes) by sodium dodecyl sulfate. J. Biochem. 106, 495-500.

Ariyoshi, T., Hasegawa, H., Nanri, Y. a. Arizono, K. (1990) Profile of hemoproteins and heme-metabolizing enzymes in rats treated with surfactants. Bull. Environ. Contam. Toxicol. 44, 369-76.

Moore, B.M. a. Flurkey, W.H. (1990) Sodium dodecyl sulfate activation of a plant polyphe-noloxidase. Effect of sodium dodecyl sulfate on enzymic and physical characteristics of purified broad bean polyphenoloxidase. J. Biol. Chem. 265, 4982-8.

Rao, R.H. a. Mansbach, C.M. II. (1990) Acid lipase in rat intestinal mucosa: physiological parameters. Biochim. Biophys. Acta. 1043, 273-80.

Solubilization and Characterization of Photosystems/Photosynthesis Pigments

Herrmann, P., Hladik, J. a. Sofrova, D. (1988) Effect of detergents on thylakoid membranes of chloroplasts. Photosynthetica 22, 411-22.

Solubilization and Characterization of Various Proteins/Protein Complexes
Hjerten, S., Sparrman, M. a. Liao, J. (1988) Purification of membrane proteins in SDS and subsequent renaturation. Biochim. Biophys. Acta 939, 476-84.

Tomich, J.M., Carson. L.W., Kanes, K.J., Vogelaar, N.J., Emerling, M.R. a. Richards, J.H. (1988) Prevention of aggregation of synthetic membrane-spanning peptides by addition of detergent. Anal. Biochem. 174, 197-203.

Bosserhoff, A., Wallach, J. a. Frank, R.W. (1989) Micropreparative separation of peptides de-rived from sodium dodecyl sulfate-solubilized proteins. J. Chromatogr. 473, 71-7.

Chakrabarty, S. (1989) Fibrin solubilizing properties of certain anionic and cationic detergents. Thromb. Res. 55, 511-9.

Welinder, B.S., Soerensen, H.H. a. Hansen, B. (1989) High-performance liquid chromato-graphic separation of membrane proteins isolated from erythrocyte ghosts. J. Chromatogr. 462, 255-68.

Sedzik, J. et al. (2002) Towards crystallization of hydrophobic myelin glycoproteins: P0 and PASII/PMP22. Protein Expression a. Purification 26, 368-77.

Protein Assays

Orsonneau, J.L., Douet, P., Massoubre, C., Lustenberger, P. a. Bernard, S. (1989) An im-proved pyrogallol red-molybdate method for determining total urinary protein. Clin. Chem. 35, 2233-6.

Harrington, C.R. (1990) Lowry protein assay containing sodium dodecyl sulfate in microtiter plates for protein determinations on fractions from brain tissue. Anal. Biochem. 186, 285-7.

DNA Preparation/DNA Assays

Csaikl, U. a. Csaikl, F. (1988) Speeding-up mitochondrial DNA preparation by a modified alkaline SDS method. J. Biochem. Biophys. Methods 17, 203-5.

Lipman, J.M. (1989) Fluorophotometric quantitation of DNA in articular cartilage utilizing Hoechst 33258. Anal. Biochem. 176, 128-31.

Morel, J., Groult, R., Cerutti, P. a. Gagnepain, J. Y. (1989) Extraction of pure high-molecularweight DNA. Fr. Demande FR 2,628,440.

Smith, G.L.F., Sansone, C. a. Socransky, S.S. (1989) Comparison of two methods for the small-scale extraction of DNA from subgingival microorganisms. Oral Microbiol. lmmunol. 4, 135-40.

Van Huynh, N., De Backer, O., Decleire, M. a. Colson, C. (1989) A procedure for the preparation of bacterial DNA that employs dimethyl sulfoxide to induce the lysis of cells. Anal. Biochem. 176, 464-7.

Immunological Determination Procedures

Smith, C.F., Musich, P.R. a. Johnson, D.A. (1989) Sodium dodecyl sulfate enhancement of quantitative immunoenzyme dot-blot assays on nitrocellulose. Anal. Biochem. 177, 212-9.

Chromatographic and Electrophoretic Separations

Cohen, A.S., Najarian, D., Smith, J.A. a. Karger, B.L. (1988) Rapid separation of DNA restriction fragments using capillary electrophoresis. J. Chromatogr. 458, 323-33.

Jira, T. a. Beyrich, T. (1988) Ion-pair HPLC of a multicomponent pharmaceutical system. Pharmazie 43, 768-71.

Dolnik, V., Liu, J., Banks, F. Jr., Novotny, M.V. a. Bocek, P. (1989) Capillary zone electrophoresis of oligonucleotides. Factors affecting separation. J. Chromatogr. 480, 321-30.

Haginaka, J., Wakai, J. a. Yamuda, H. (1989) Direct serum injection in micellar liquid chromatography. Recovery of serum proteins and assays of hydrophilic drugs. J. Chromatogr. 488, 341-8.

Liu, J., Banks, J.F. Jr. a. Novotny, M. (1989) High-speed micellar electrokinetic capillary chromatography of the common phosphorylated nucleosides. J. Microcolumn Sep. 1,136-41.

Oshima, T., Sagara, K., Tong, Y., Zhang, G. a. Chen, Y. (1989) Application of ion-pair high-performance liquid chromatography for analysis of hyoscyamine and scopolamine in solanaceous crude drugs. Chem. Pharm. Bull. 37, 2456-8.

Scher, M.G., Resneck, W.G. a. Bloch, R.J. (1989) Stabilization of immobilized lectin columns by crosslinking with glutaraldehyde. Anal. Biochem. 177, 168-71.

Wallingford, R.A. a. Ewing, A.G. (1989) Separation of serotonin from catechols by capillary zone electrophoresis with electrochemical detection. Anal. Chem. 61, 98-100.

Kawasaki, H. a. Suzuki, K. (1990) Separation of peptides dissolved in a sodium dodecyl sulfate solution by reversed-phase liquid chromatography: removal of sodium dodecyl sulfate from peptides using an ion-exchange precolumn. Anal. Biochem. 186, 264-8.

Warlow, R.S. a. Bernard, C.C.A. (1990) Improved detection of lymphocyte membrane proteins in purified form and as a crude mixture using native and denaturing polyacrylamide gel electrophoresis by optimization of Coomassie Brilliant Blue and silver staining. Electrophoresis 11, 53-60.

Dover, L.G. a. Ratledge, C. (1996) Identification of a 29 kDa protein in the envelope of Mycobacterium smegmatis as a putative ferri-exochelin receptor. Microbiology 142, 1521-30

Churchward, M.A. et al. (2005) Enhanced detergent extraction for analysis of membrane proteomes by two-dimensional gel electrophoresis. Proteome Sci. 3:5.
Liu, R. et al. (2009) Characterization of fluorescent sterol binding to purified human NPC1. J. Biol. Chem. 284, 1840-52.

Further Applications

Li, J.K.K., Johnson, T., Yang, Y. Y. a. Shore, V. (1989) Selective separation of virus proteins and double-stranded RNAs by SDS-potassium chloride precipitation. J. Virol. Methods 26, 3-15.

Neu, T.R. (1996) Significance of bacterial surface-active compounds in interaction of bacteria with interfaces. Microbiol. Reviews (American Society for Microbiology), 151-166

Piret, J. et al. (2002) Comparative study of mechanisms of Herpes simplex virus inactivation by sodium lauryl sulfate and N-lauroylsarcosine. Antimicrob. Agents Chemother. 46, 2933-42.

Owoyomi, O. et al. (2005) Interaction between sodium dodecylsulphate and Triton X-100: Molecular properties and kinetics investigations. J. Applied Sciences 5, 729-34.



Top
Close window
SERVA Market Square: March - June 2020

• Vertical Protein Electrophoresis
• Horizontal Protein Electrophoresis
• Western Blotting
• Fluorescent  Dyes
• DNA/RNA Electrophoresis
• Fluorescence Labelling
• Cell based Assays
• Enzymes
• Detergents
• Protease- and Phosphatase Inhibitors

  → This way to the Special Offer

Close window
Product of the Month May:
CoolRack™

CoolRack™-  Optimal Sample Handling at any Temperature

→ This way to the Special Offer

SERVA InfoMail - Get the latest information

Close window

When subscribing to »SERVA InfoMail« you will receive information about the latest product release, special promotions, new jobs at SERVA and more. This service is, of course, free of charge.
You may remove your name any time from the list of recipients.

Quick Order

Close window

Using the Quick Order field, you can add a product to your shopping cart with just one click. All you have to do: enter the Cat.No. as shown in our catalog in the format xxxxx.yy and click the Go!-Button.