Preparation of Barley Storage Protein, Hordein, for Analytical Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

Hans Doll, Bente Andersen

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    The extraction, reduction, and alkylation of barley hordein for routine electrophoresis in sodium dodecyl sulfate-polyacrylamide gels were studied to set up a simple preparation procedure giving well-resolved bands in the electrophoresis gel. Hordein was extracted from single crushed seeds or flour by aqueous 50% propan-2-ol containing a Tris-borate buffer, pH 8.6. The presence of the buffer facilitates the consecutive complete reduction of the extracted protein in the alcohol. Reduction and alkylation in the buffer containing propan-2-ol give sharper bands in the electrophoresis than reduction in a buffer without propan-2-ol but containing sodium dodecyl sulfate.
    Original languageEnglish
    JournalAnalytical Biochemistry
    Volume115
    Issue number1
    Pages (from-to)61-66
    ISSN0003-2697
    DOIs
    Publication statusPublished - 1981

    Fingerprint Dive into the research topics of 'Preparation of Barley Storage Protein, Hordein, for Analytical Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis'. Together they form a unique fingerprint.

    Cite this