APPLICABILITY OF CAPILLARY ELECTROPHORESIS IN PROTEIN SEPARATIONS WITH REGARD TO WHEAT AND WHEAT ANALOGOUS PROTEINS

Abstract

High-performance capillary electrophoresis (HPCE), among other analytical techniques (e.g. acid polyacrylamide gel electrophoresis, sodium dodecyl sulphate polyacrylamide gel electrophoresis and reversed-phase high-performance liquid chromatography) [1]-[4] is more and more widely used also in the field of separation of cereal proteins [5]-[18]. HPCE is versatile, easy to automate, does not need toxic reagents or long analysis time, but requires only small sample size, small amount of buffer and provides high-resolution separations. So this analytical technique is particularly applicable for studying the fine structure of the composition of wheat proteins. Capillary electrophoresis has been used at our department for the determination of the fine structure of different wheat protein fractions [19]. Differences between the various wheat cultivars and changes during grain maturation process have also been studied using a home-built capillary electrophoretic system [20]. The same system has been used to investigate the electrophoretic properties of a gliadin analogous protein (BM180 - a basement membrane protein with a potential autoantigen role) [21]. The more strictly controllable nature of an automated system (especially the temperature control of the capillary) allows the use of higher voltages, so separation time decreases and resolution increases. Purchasing an automated capillary electrophoretic system we gained an opportunity to compare the two electrophoretic systems also in the field of wheat protein analyses. The aim of present work was to give an impression of the work done by capillary electrophoresis at our department.