Separation of hordein proteins from european barley by high-performance liquid chromatography: Its application to the identification of barley cultivars

Summary High-performance liquid chromatography using either reversed phase or anion-exchange techniques was used for the fractionation of hordein proteins extracted from European barley. A reversed phase method is presented which utilises an Ultrapore column packed with a wide pore (30 nm) C-3 alkylbonded silica support. Using this method up to 20 components may be separated in 54 min. Elution profiles were found to be reproducible. A further method using rapid anion-exchange chromatography indicated that up to 13 components may be separated, a number which is comparable to that found with electrophoresis. The separation of proteins extracted from different barley cultivars indicated that on the basis of elution profiles high-performance liquid chromatography using either reversed phase or anion-exchange offers considerable potential as a method for barley cultivar identification.