Electrophoresis sodium dodecyl sulfonate

Eiectrophoresis. Electrophoresis is widely practiced on biopolymers (266-268) for the determination of molecular weights of proteins and their subunits. Typically, a polyacrylamide bed is used to separate or characterize these solutes under the influence of an electric field, on the basis of charge and molecular size. The proteins are frequently denatured with sodium dodecyl sulfonate (SDS), and these subunit-SDS complexes are separated on the basis of molecular size. A densitometer employing a soft laser scanning device is commercially available to automate the data-reduction process (269). 

The method of Kato and Nakai (27) for determining protein surface hydrophobicity was adapted for evaluating procyanidin binding to BSA and Gl. The procedure is based on the fact that the fluorescence quantum yield of cis-parinaric acid increases 40-fold when cis-parinaric acid enters a hydrophobic environment from a hydrophilic environment. The digestion of BSA by trypsin in the presence of procyanidin dimer, procyanidin trimer and black bean procyanidin polymer was evaluated by discontinuous sodium dodecyl sulfate (SDS) slab gel electrophoresis and a picryl sulfonic acid (TNBS) assay (28). 

PL PVC Q RPC S SM SP SDS SDS-PAGE TEAE TAM Ve V0 vs Vt X y reversible complex ptotein-ligand poly vinyl chloride quaternary amine reverse phase chromatography Sulfonate Sulfomethyl Sulfopropyl sodium dodecyl sulphate sodium dodecyl sulphate - polyacrylamide gel electrophoresis Triethylaminoethyl Trimethylaminomethyl elution volume interstitial volume of the porous matrix total solvent volume within the pores total column volume solute concentration in the original solution solute concentration in the extract... 

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