CTAB-PAGE

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The CTAB-PAGE is a biochemical method for the separation of proteins according to their molecular weight in a polyacrylamide gel electrophoresis (PAGE) using the surfactant cetyltrimethylammonium bromide (CTAB).

properties

The CTAB-PAGE is suitable for the separation of proteins with many positive charges or glycosylated membrane proteins . In contrast to the commonly used SDS-PAGE , the proteins loaded with the cationic surfactant CTAB migrate to the cathode (minus pole). Alternatively, the BAC-PAGE with 16-benzyldimethylhexadecylammonium chloride (16-BAC) can be used instead of CTAB as the PAGE with a cationic surfactant . If the samples are not heated with the sample buffer and no reducing agent for disulfide bridges such as mercaptoethanol , dithiothreitol or dithioerythritol has been added, the native conformation and biological activity of the proteins is partially retained.

Individual evidence

  1. ↑ RJ Brown, N. Kinkl, M. Beer, M. Ueffing: Two-dimensional electrophoresis of membrane proteins. In: Analytical and bioanalytical chemistry. Volume 389, Number 4, October 2007, pp. 1033-1045, doi : 10.1007 / s00216-007-1514-6 , PMID 1768023 .
  2. ↑ Engelbert Buxbaum: Cationic electrophoresis and electrotransfer of membrane glycoproteins. In: Analytical Biochemistry. Vol. 314, No. 1, 2003, pp. 70-76, PMID 12633604 , doi : 10.1016 / S0003-2697 (02) 00639-5 .
  3. ↑ Dianne T. Akin, Raymond Shapira, Joseph M. Kinkade Jr .: The determination of molecular weights of biologically active proteins by cetyltrimethylammonium bromide-polyacrylamide gel electrophoresis. In: Analytical Biochemistry. Vol. 145, No. 1, 1985, pp. 170-176, PMID 4003759 , doi : 10.1016 / 0003-2697 (85) 90343-4 .
  4. ^ RJ Simpson: CTAB-PAGE. In: Cold Spring Harbor protocols. Volume 2010, number 4, April 2010, p. Pdb.prot5412, doi : 10.1101 / pdb.prot5412 , PMID 20360366 .
  5. ↑ Joachim Hartinger, Katinka Stenius, Dagmar Högemann, Reinhard Jahn : 16-BAC / SDS-PAGE: a two-dimensional gel electrophoresis system suitable for the separation of integral membrane proteins. In: Analytical Biochemistry. Vol. 240, No. 1, 1996, pp. 126-133, PMID 8811889 , doi : 10.1006 / abio.1996.0339 .