Bushey M M, Jorgenson J W
Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290.
J Chromatogr. 1989 Oct 20;480:301-10. doi: 10.1016/s0021-9673(01)84299-0.
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.
研究了一种利用高浓度两性离子缓冲添加剂改善毛细管区带电泳中蛋白质分离的方法。在pH约为7.0和9.0的缓冲液中，使用溶菌酶和α-胰凝乳蛋白酶原A作为测试蛋白，在未处理的熔融石英毛细管中进行实验。将含两性离子的缓冲液与含高离子盐浓度的缓冲液以及含高离子盐和高两性离子浓度组合的缓冲液进行比较。在含有三甲基甘氨酸和硫酸钾的pH 7缓冲液中，两种测试蛋白在不到30分钟的时间内获得了超过100,000个理论塔板数。讨论了该技术与用于防止蛋白质吸附的其他方法相比的优缺点。
