Na-Dodecylsulfat (SDS) gehört zu den stärksten Solubilisatoren für integrale Membranproteine. 

SDS hat den Vorteil, dass es eine Aggregation verhindert, führt aber meist zu einer Denaturierung der Membranproteine. Einige der mit SDS solubilisierten Membranproteine, die sich in einem denaturierten Zustand befinden, z. B. eine 5'-Nukleotidase oder eine Neuraminidase, wurden erfolgreich renaturiert.

Na-Dodecylsulfat ist ein potentes fibrinolytisches Tensid.

SDS ist von Bedeutung bei der Isolierung von DNA ohne Phenol-Extraktion. Es hat sich auch bei der Abtrennung von Virusproteinen und doppelsträngigen RNAs bewährt; eine SDS-KCl-Fällung ermöglicht eine schnelle und selektive Trennung in einem Schritt. 

Verschiedene Proteinassays können durch Modifikation mit Na-Dodecylsulfat verbessert werden. 

Na-Dodecylsulfat wird bevorzugt in der Polyacrylamid-Gelelektrophorese zur Auftrennung von Proteinen und Peptiden eingesetzt und wird häufig zur Optimierung chromatographischer Trennungen verwendet. 

Synonyme: SDS, Natriumlaurylsulfat 

CAS-Registriernummer: [151-21-3] 

Molekulare Formel: C₁₂H₂₅O₄S . Na 

Relative Molmasse (M_r): 288,4 

Klassifizierung: Anionisches Tensid

 

Literaturangaben:

- Kritische mizellare Konzentration (CMC): 8,1 mM

- Aggregationszahl (Na): 60 - 62

- Krafft-Punkt (TK): 9 °C

- Hydrophil-Lipophilie-Gleichgewicht (HLB): 40

BibliographIE

Charakterisierung und Bestimmung von Enzymen

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.

Solubilisierung und Charakterisierung von Photosystemen/Photosynthesepigmenten

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.

Immunologische Bestimmungsverfahren

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.

Chromatographische und elektrophoretische Trennungen

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.

Weitere Applikationen

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.