Origin of multiple bands of proteins on sodium dodecyl sulphate-polyacrylamide gel electrophoresis--intermolecular disulphide cross-linking due to the presence of oxidizing components in the reducing agent.
The presence of oxidized products in the reducing agent used in sodium dodecyl sulphate-polyacrylamide gel electrophoresis is shown to yield multiple bands from otherwise homogeneous RNase A. The role of oxidized products in generating multiple bands is elucidated by using varying proportions of oxidized and reduced glutathione in a mixture as a reducing agent.
Kumar
T K
TK
Centre for Cellular and Molecular Biology, Hyderabad, India.
Prasad
V V
VV
Pandit
M W
MW
D003432:Cross-Linking Reagents; D004220:Disulfides / Q000737:chemistry*; D004229:Dithiothreitol; D004591:Electrophoresis, Polyacrylamide Gel; D005978:Glutathione / Q000737:chemistry*; D008623:Mercaptoethanol; D010084:Oxidation-Reduction; D012259:Ribonuclease, Pancreatic / Q000032:analysis*
D003432:Cross-Linking Reagents; D004220:Disulfides; D008623:Mercaptoethanol; D012259:Ribonuclease, Pancreatic; D005978:Glutathione; D004229:Dithiothreitol