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

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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.

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Authors and Affiliations

  1. Department of Life Sciences, Trent Polytechnic, Clifton Lane, NG11 8NS, Nottingham, UK

    C. E. Wingad, M. Iqbal & M. Griffin

  2. Lady Bay Works, Kelco Int. Ltd., Girvan, Ayrshire

    F. J. Smith

Authors
  1. C. E. Wingad
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  2. M. Iqbal
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  3. M. Griffin
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  4. F. J. Smith
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Wingad, C.E., Iqbal, M., Griffin, M. et al. Separation of hordein proteins from european barley by high-performance liquid chromatography: Its application to the identification of barley cultivars. Chromatographia 21, 49–54 (1986). https://doi.org/10.1007/BF02310595

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  • DOI: https://doi.org/10.1007/BF02310595

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