Capillary electrophoresis of proteins in buffers containing high concentrations of zwitterionic salts

✍ Scribed by Michelle M. Bushey; James W. Jorgenson

• Publisher: Elsevier Science
• Year: 1989
• Tongue: English
• Weight: 613 KB
• Volume: 480
• Category: Article
• ISSN: 1873-3778
• DOI: 10.1016/s0021-9673(01)84299-0

✦ Synopsis

A method for improving protein separations in capillary zone electrophoresis utilizing high concentrations of zwitterionic buffer additives was examined. Lysozyme and cc-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.