title: Binding of lithium dodecyl sulfate to polyacrylamide gel at 4 degrees C perturbs electrophoresis of proteins.
abstract: Although polyacrylamide gel has no affinity to lithium dodecyl sulfate (LDS) at 25 degrees C, the gel maximally binds 17 mg of LDS per gram dry weight at 4 degrees C. When polyacrylamide gel electrophoresis is carried out at 4 degrees C in the presence of LDS instead of sodium dodecyl sulfate (SDS) using a continuous buffer system, migration of proteins with lower molecular weight is accelerated as a result of the deficiency of LDS in the frontal region of the gel. When the gel is saturated with LDS, electrophoresis in the presence of LDS at 4 degrees C shows a resolution higher than that of SDS-polyacrylamide gel electrophoresis at 25 degrees C.
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D011506:Proteins / Q000032:analysis*; D012967:Sodium Dodecyl Sulfate; D013696:Temperature
chemical_list: D011506:Proteins; D012967:Sodium Dodecyl Sulfate; C028913:dodecyl sulfate