Removal of sodium dodecyl sulphate from proteins isolated by sodium dodecyl sulphate polyacrylamide gel electrophoresis.
A procedure is described for the removal of sodium dodecyl sulphate (SDS) from proteins isolated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). The proteins separated by SDS-PAGE were stained with Coomassie Blue and extracted with Tris-HCl buffer containing SDS. The obtained extracts were subjected to gel permeation chromatography in an acidic aqueous acetonitrile solution. The procedure allows purification of the isolated proteins not only from SDS, but also from Coomassie Blue, buffer salts and other small molecular weight contaminants.
Kaplan
B
B
Heller Institute of Medical Research, Chaim Sheba Medical Center, Sackler Medical School, Tel-Aviv University, Israel.
Pras
M
M
D000097:Acetonitriles; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007782:Lactoglobulins / Q000302:isolation & purification; D009113:Muramidase / Q000302:isolation & purification; D010047:Ovalbumin / Q000302:isolation & purification; D011506:Proteins / Q000302:isolation & purification*; D012710:Serum Albumin, Bovine / Q000302:isolation & purification; D000685:Serum Amyloid A Protein / Q000302:isolation & purification; D012967:Sodium Dodecyl Sulfate; D014269:Trifluoroacetic Acid
D000097:Acetonitriles; D007782:Lactoglobulins; D011506:Proteins; D000685:Serum Amyloid A Protein; D012710:Serum Albumin, Bovine; D012967:Sodium Dodecyl Sulfate; D010047:Ovalbumin; D014269:Trifluoroacetic Acid; D009113:Muramidase; C032159:acetonitrile