Separation and identification of hen egg protein isoforms using SDS-PAGE and 2D gel electrophoresis with MALDI-TOF mass spectrometry

Vassilios Raikos, Rasmus Hansen, Lydia Campbell, Stephen R. Euston

    Research output: Contribution to journalArticle

    60 Citations (Scopus)

    Abstract

    Knowledge of the chemical composition and physicochemical properties of native egg white and yolk is necessary to interpret the functional and biological properties attributed to specific egg components. To date, many of the proteins located in this complex biological fluid remain uncharacterised, if not unknown. High-resolution techniques for proteome analysis, including SDS-PAGE and 2-dimensional (2D) gel electrophoresis, combined with mass spectrometry, were employed to separate and identify several protein components in hen's egg. An advanced and sensitive glycoprotein staining kit was used to detect the presence of glycosylated proteins in the egg samples. Numerous spots were revealed when a mixture of egg white and yolk was subjected to 2D gel electrophoresis. Several of the already known egg proteins were identified. Isoforms of ovalbumin and conalbumin were visualised. The presence of FLJ 10305 and Fatso proteins in the proteome of Gallus domesticus was also confirmed. © 2005 Elsevier Ltd. All rights reserved.

    Original languageEnglish
    Pages (from-to)702-710
    Number of pages9
    JournalFood Chemistry
    Volume99
    Issue number4
    DOIs
    Publication statusPublished - 2006

    Keywords

    • 2-Dimensional gel electrophoresis
    • Glycoprotein stain kit
    • Hen egg proteins
    • MALDI-TOF
    • Proteomic
    • SDS-PAGE

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