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Urea-extractable protein from human epidermis

J Baynes, M Levine

    Biochimica Et Biophysica Acta
    |July 19, 1976
    PubMed
    Summary
    This summary is machine-generated.

    This study characterizes a major protein fraction from human epidermis, revealing a high molecular weight and a non-protein component. The findings detail its structure, including disulfide linkages and the dissociation of aggregates in urea.

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    Area of Science:

    • Biochemistry
    • Dermatology
    • Proteomics

    Background:

    • Human epidermis contains complex protein structures crucial for skin barrier function.
    • Previous research has identified various epidermal proteins, but their precise composition and interactions remain areas of investigation.

    Purpose of the Study:

    • To characterize the major protein fraction extracted from human epidermis using urea.
    • To elucidate the structural and compositional properties of this protein fraction.

    Main Methods:

    • Urea extraction of protein from human epidermis.
    • Determination of molecular weight, copper content, and non-protein moieties.
    • Analysis of interchain disulfide linkages using polyacrylamide gel electrophoresis (PAGE) in sodium dodecyl sulfate (SDS) with and without beta-mercaptoethanol.

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  • Investigation of urea's effect on protein aggregates using PAGE in the presence and absence of 6 M urea.

    • Main Results:

    • The major protein fraction exhibits a high molecular weight of approximately 600,000 Da.
    • A copper content of 0.03% was detected, suggesting a minimum molecular weight of 212,000 Da.
    • Evidence for a non-protein moiety was found through various analyses, excluding urocanic acid and RNA.
    • Interchain disulfide linkages were identified, and PAGE indicated that urea dissociates protein aggregates.

    Conclusions:

    • The characterized protein fraction is a large, complex structure with significant non-protein components.
    • Disulfide bonds play a role in maintaining the protein's structural integrity.
    • Urea effectively disaggregates this protein fraction, aiding in its structural analysis.