glassmicrofluidicchipbasedsodiumdodecylsulfatenongelsievingelectrophoresisfordeterminingmolecularweightsofimmunoglobulinfragments

Abstract

The concentrations of dextran sieving matrix and running buffer were optimized. Under the optimized conditions (10% (w/v) dextran, 0.1% SDS, 10% glycerol, 0.2 mol/L Tris-boric acid, pH 8.3), six standard proteins could be efficiently separated using sodium dodecyl sulfate (SDS)-nongel sieving electrophoresis on home-made glass microfluidic chip. The relative standard deviations (RSDs) for migration time were lower than 0.50%. A good linear relationship (r =0.994) was built between the migration time of each protein and the logarithm of its molecular weight (logMr). Using the chip-based electrophoretic separation system, the molecular weights of different fragments of immunoglobulin G after different treatments were measured, and the results matched the facts