Capillary electrophoresis of proteins in buffers containing high concentrations of zwitterionic salts.
A method for improving protein separations in capillary zone electrophoresis utilizing high concentrations of zwitterionic buffer additives was examined. Lysozyme and alpha-chymotrypsinogen A were used as test proteins in untreated fused-silica capillaries in buffers of pH ca. 7.0 and 9.0 The zwitterion-containing buffers were compared with buffers containing high ionic salt concentrations and a buffer containing a combination of high ionic salt and high zwitterion concentrations. Over 100,000 theoretical plates were obtained in less than 30 min. for both test proteins in a pH 7 buffer containing both trimethylglycine and potassium sulfate. The advantages and disadvantages of this technique compared with those of other methods used to prevent protein adsorption are discussed.
Bushey
M M
MM
Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290.
Jorgenson
J W
JW
D000818:Animals; D002919:Chymotrypsinogen / Q000032:analysis; D004586:Electrophoresis / Q000379:methods*; D009113:Muramidase / Q000032:analysis; D009994:Osmolar Concentration; D011506:Proteins / Q000032:analysis*; D013050:Spectrometry, Fluorescence
D011506:Proteins; D002919:Chymotrypsinogen; D009113:Muramidase