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Related Experiment Videos

Human epidermal transglutaminase. Preparation and properties.

H Ogawa, L A Goldsmith

    The Journal of Biological Chemistry
    |December 10, 1976
    PubMed
    Summary

    Researchers purified a transglutaminase from human epidermis. This enzyme cross-links fibrinogen and requires calcium or strontium for activity, with activation influenced by heat or DMSO.

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    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Transglutaminases are enzymes involved in protein cross-linking.
    • Human hair follicle-free epidermis is a source of various enzymes.

    Purpose of the Study:

    • To purify and characterize a transglutaminase from human hair follicle-free epidermis.
    • To investigate the enzyme's activity, substrate specificity, and activation mechanisms.

    Main Methods:

    • Purification using gel filtration and ion exchange chromatography.
    • Enzyme activity assays using fibrinogen, casein, and putrescine.
    • Molecular weight determination via SDS-PAGE and discontinuous gel electrophoresis.
    • Analysis of activation by heat and dimethylsulfoxide in the presence of calcium or strontium.

    Main Results:

    • A transglutaminase was purified to homogeneity.
    • The enzyme cross-linked Factor XIII-free fibrinogen into gamma dimers and alpha polymers.
    • Enzyme activity was dependent on calcium or strontium ions.
    • Activity was enhanced by heating or dimethylsulfoxide treatment in the presence of calcium.
    • Kinetic parameters (Km) for casein and putrescine were similar for native and activated enzyme forms.

    Conclusions:

    • A novel transglutaminase from human epidermis was identified and characterized.
    • The enzyme's cross-linking activity and dependence on divalent cations were established.
    • Specific activation conditions were identified, though the precise mechanism requires further investigation.

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