Abstract
Sodium dodecylsulphate (SDS) consists of an aliphatic chain of 12 C atoms to which at one end a sulphate residue is bound. It forms complexes with both the polar and non- polar amino acid residues of proteins irrespective of their sizes and shapes, leaving the primary structure uninfluenced. In electrophoresis SDS is used:
-
a)
to separate (enzyme) proteins into their monomeric constituents,
-
b)
to estimate the molecular mass of unfolded (and reduced) polypeptides, and
-
c)
to keep membrane proteins in a solubilized state.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Pitt-Rivers R, Impiombato FSA (1968) Biochem J109: 825–830
Reynolds JA, Tanford C (1970) Proc. Natl Acad Sei USA 66:1002–1007
Reynolds JA (1970) J Biol Chem 245:5161–5165
Nelson CA (1971) J Biol Chem 246:3895–3901
5.Segrest JP, Jackson RL, Andrews EP, Marchesi VT (1971) Biochem Biophys Res Comm 44:
390–395
Shapiro AL, Vinuela E, Maizel JV (1967) Biochem Biophys Res Comm 28:815–820
Wachneldt TV (1971) Anal Biochem 43:306–312
Lambin P (1978) Anal Biochem 85:114–125
Maizel JV (1971) Methods in Virology 5:179–246
Weber K, Osborn M (1969) J Biol Chem 244:4406–4412
Dunker AK, Rueckert RR (1969) J Biol Chem 244:5074–5080
Laemmli UK (1970) Nature 227:680–685
Grefrath SP, Reynolds JA (1974) Proc Nad Acad Sei USA 71:3913–3916
Barker GA, Cotman CW (1972) J Biol Chem 247:5856–5861
Anderson BL, Berry RW, Telser A (1983) Anal Biochem 32:365–375
King J, Laemmli U (1971) J Mol Biol 62:465–477
Lambin P, Rochu D, Fine JM (1976) Anal Biochem 74:567–575
Rüchel R, Mesecke S, Wolfrum DI, Neuhoff, V (1974) Hoppe-Seyler’s Z Physiol. Chem 355: 997–1020
Rothe GM (1982) Electrophoresis 3:255–262
Lasky M (1978) Protein molecular weight determination using Polyacrylamide gradient gels in the presence and absence of sodium dodecyl sulfate. In: Catsimpoolas N (ed), Electrophoresis ’78, North Holland, Amsterdam, pp 195–210
Poduslo JF, Rodbard D (1980) Anal Biochem 101:394–406
Lacks SA, Springhorn SS, Rosenthal AL (1979) Anal Biochem 100:357–363
Lacks SA, Springhorn SS (1980) J Biol Chem 255:746–773
Manrow RE, Dottin RP (1980) Proc Natl Acad Sei 77:730–734
Dottin RP, Manrow RE, Fishel BR, Ankermann SL, Culleton, I.L (1979) Localization of enzymes in denaturing Polyacrylamide gels. In: Wu R (ed) Methods in enzymology vol 68. Academic Press, New York London Toronto Sydney San Francisco, pp 513–529
Weber K, Kuter DD (1971) J Biol Chem 246:4504–4509
Rosenthal AL, Lacks SA (1977) Anal Biochem 80:76–90
Blank A, Sugiyama RH, Dekker CA (1982) Anal Biochem 120:267–275
Blank A, Silber JR, Thelen MP, Dekker CA (1983) Anal Biochem 135:423–430
Thelen MP, Blank A, McKeon TA, Dekker CA (1982) Fed Proc 41:1203
Matheka HD, Enzmann PJ, Bachrach HL, Migel B (1977) Anal Biochem 81:9–17
Margulies MM, Tiffany HL (1984) Anal Biochem 136:309–313
Dohnal JC, Garvin IE (1979) Biochim Biophys Acta 576:393–403
Zaman Z, Verwilghen RL (1979) Anal Biochem 100: 64–69
Hager DA, Burgess RR (1980) Anal Biochem 109:76–86
Russell RRB (1979) Anal Biochem 97:173–175
Dulaney JT, Touster O (1970) Biochim Biophys Acta 196:29–34
Huet J, Sentenac A, Fromageot P (1978) FEBS Letters 94:28–32
Spanos A, Sedgwick SG, Yarranton GT, Hübscher U, Banks GR (1981) Nucleic Acids Res 9:5919–5925
Ohta Y, Oguva Y, Wada A (1966) J Biol Chem 241:5919–5925
Takagi T, Toda H, Isemura T (1971) Bacterial and mold amylases. In: Boyer PD (ed) The Enzymes 3rd ed. Vol 5, Academic Press, New York, pp 235–271
Thoma JA, Spradlin JE, Dyget S (1971) Plant and animal amylases. In: Boyer PD (ed) The Enzymes 3rd ed. Vol 5, Academic Press, New York, pp 115–189
Olive C, Levy HR (1971) J Biol Chem 246:2043–2046
Appella E, Markert CL (1961) Biochem Biophys Res Commun 6:171–176
Blank A, Dekker CA (1982) Biochem 20:2261–2267
Anfinsen CB (1962) Brookhaven Symp Biol 15:184–198
Martin CJ (1964) Biochemistry 3:1635–1643
Westhead EW (1964) Biochemistry 3:1062–1068
Kaufmann BT (1963) Biochem Biophys Res Commun 10:449–453
Kaufmann BT (1968) J Biol Chem 243: 6001–6008
Perkins JP, Bertino JR (1965) Biochemistry 4: 847–853
52.Stadtman ER (1960) Advan Enzymol 28:41–154
Schneidermann LJ (1965) Biochem Biophys Res Commun 20:763–767
Weinbaum G, Markman R (1966) Biochim Biophys Acta 124: 207–209
Rothe GM, Maurer WD (1986). One-dimensional PAA-gel electrophoretic techniques to separate functional and denatured proteins. In: Dunn MJ (ed) Electrophoresis of Proteins. Wright, Bristol, pp 37–140
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1994 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Rothe, G.M. (1994). Sodium Dodecylsulphate Electrophoresis. In: Electrophoresis of Enzymes. Springer Labmanual. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79069-0_4
Download citation
DOI: https://doi.org/10.1007/978-3-642-79069-0_4
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-79071-3
Online ISBN: 978-3-642-79069-0
eBook Packages: Springer Book Archive