• myGriffith
    • Staff portal
    • Contact Us⌄
      • Future student enquiries 1800 677 728
      • Current student enquiries 1800 154 055
      • International enquiries +61 7 3735 6425
      • General enquiries 07 3735 7111
      • Online enquiries
      • Staff phonebook
    View Item 
    •   Home
    • Griffith Research Online
    • Journal articles
    • View Item
    • Home
    • Griffith Research Online
    • Journal articles
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

  • All of Griffith Research Online
    • Communities & Collections
    • Authors
    • By Issue Date
    • Titles
  • This Collection
    • Authors
    • By Issue Date
    • Titles
  • Statistics

  • Most Popular Items
  • Statistics by Country
  • Most Popular Authors
  • Support

  • Contact us
  • FAQs
  • Admin login

  • Login
  • Rapid purification of EGFP, EYFP, and ECFP with high yield and purity

    Author(s)
    McRae, SR
    Brown, CL
    Bushell, GR
    Griffith University Author(s)
    Brown, Chris L.
    Bushell, Gillian R.
    McRae, Shelley R.
    Year published
    2005
    Metadata
    Show full item record
    Abstract
    Most current high throughput puriWcation procedures for the green Xuorescent protein (GFP) suVer from poor yields and low purity. An improved puriWcation procedure that delivers highly pure protein (>95% homogeneity) in high yields (>70% of the initial Xuorescent protein content) has been developed. The puriWcation procedure requires only two steps: the cell lysate is heated to 60 Í for 4min in ammonium sulfate and triethylamine, followed by hydrophobic interaction chromatography using isopropanol during the elution phase. The resulting pure product exhibits the same Xuorescence proWle as the crude sample. This procedure has ...
    View more >
    Most current high throughput puriWcation procedures for the green Xuorescent protein (GFP) suVer from poor yields and low purity. An improved puriWcation procedure that delivers highly pure protein (>95% homogeneity) in high yields (>70% of the initial Xuorescent protein content) has been developed. The puriWcation procedure requires only two steps: the cell lysate is heated to 60 Í for 4min in ammonium sulfate and triethylamine, followed by hydrophobic interaction chromatography using isopropanol during the elution phase. The resulting pure product exhibits the same Xuorescence proWle as the crude sample. This procedure has been demonstrated on three commercial variants of GFP from Aequorea victoria, enhanced green, enhanced yellow, and enhanced cyan Xuorescent protein (Becton-Dickinson). The yield and purity of material are superior to other recently described methods.
    View less >
    Journal Title
    Protein Expression and Purifcation
    Volume
    41
    Publisher URI
    http://www.elsevier.com/wps/find/journaldescription.cws_home/622935/description#description
    DOI
    https://doi.org/10.1016/j.pep.2004.12.030
    Copyright Statement
    © 2005 Elsevier : Reproduced in accordance with the copyright policy of the publisher : This journal is available online - use hypertext links.
    Subject
    Biochemistry and cell biology
    Other biological sciences
    Publication URI
    http://hdl.handle.net/10072/4975
    Collection
    • Journal articles

    Footer

    Disclaimer

    • Privacy policy
    • Copyright matters
    • CRICOS Provider - 00233E

    Tagline

    • Gold Coast
    • Logan
    • Brisbane - Queensland, Australia
    First Peoples of Australia
    • Aboriginal
    • Torres Strait Islander