ORIGIN OF MULTIPLE BANDS OF PROTEINS ON SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL-ELECTROPHORESIS - INTERMOLECULAR DISULFIDE CROSS-LINKING DUE TO THE PRESENCE OF OXIDIZING COMPONENTS IN THE REDUCING AGENT
Tks. Kumar et al., ORIGIN OF MULTIPLE BANDS OF PROTEINS ON SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL-ELECTROPHORESIS - INTERMOLECULAR DISULFIDE CROSS-LINKING DUE TO THE PRESENCE OF OXIDIZING COMPONENTS IN THE REDUCING AGENT, Journal of biochemical and biophysical methods, 28(3), 1994, pp. 243-247
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 oxidiz
ed products in generating multiple bands is elucidated by using varyin
g proportions of oxidized and reduced glutathione in a mixture as a re
ducing agent.