Further purification of epidermal growth factor by high-performance liquid chromatography

Lynn M. Matrisian, Brent R. Larsen, Joanne S. Finch, Bruce E. Magun

    Research output: Contribution to journalArticlepeer-review

    56 Scopus citations

    Abstract

    Epidermal growth factor (EGF) purified by the method of Savage and Cohen (J. Biol. Chem. 247, 7601-7611 (1972) using DEAE-cellulose chromatography as the final purification step was further resolved into two major uv-absorbing components by reverse-phase high-performance liquid chromatography (HPLC). Both components, referred to as α-EGF and β-EGF, competed with 125I-labeled EGF for the EGF receptor, induced premature eye opening in neonatal mice, and had an amino acid composition similar to that published by Savage et al. (J. Biol. Chem.247, 7612-7621 (1972). β-EGF migrated slightly faster than α-EGF during sodium dodecyl sulfate-urea-polyacrylamide gel electrophoresis. α-EGF was fourfold more potent than β-EGF and was 10-fold more potent than DEAE-purified EGF in stimulating DNA synthesis in quiescent Rat-1 cells. HPLC purification of EGF can replace the DEAE-cellulose chromatography step currently used and produces a more potent and less heterogeneous EGF species.

    Original languageEnglish (US)
    Pages (from-to)339-351
    Number of pages13
    JournalAnalytical Biochemistry
    Volume125
    Issue number2
    DOIs
    StatePublished - Sep 15 1982

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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