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Related Experiment Videos

Human epidermal transamidase.

L A Goldsmith, C M Martin

    The Journal of Investigative Dermatology
    |May 1, 1975
    PubMed
    Summary
    This summary is machine-generated.

    Human epidermal transamidase activity was investigated, revealing an enzyme that incorporates putrescine into proteins. This calcium-dependent enzyme shows broad pH activity and functions similarly to other transamidases.

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    Area of Science:

    • Biochemistry
    • Dermatology
    • Enzymology

    Background:

    • Human epidermal proteins may contain epsilon-(gamma-glutamyl) lysine covalent bonds.
    • Transamidase activity in human hair-free epidermis was previously uncharacterized.

    Purpose of the Study:

    • To investigate transamidase activity in human hair-free epidermis.
    • To characterize the properties of the epidermal transamidase enzyme.

    Main Methods:

    • Studied putrescine incorporation into alpha-casein using callus enzyme.
    • Partially purified the enzyme and determined its molecular weight via gel filtration.
    • Assessed enzyme activity across a wide pH range and determined Km for putrescine.

    Main Results:

    Related Experiment Videos

  • Identified a calcium-dependent enzyme in callus catalyzing putrescine incorporation, inhibited by iodoacetamide.
  • Partially purified enzyme (50-fold) with an apparent molecular weight of 50,000-55,000 daltons.
  • Enzyme exhibited broad pH activity up to 10.4, with increased activity and stable Km for putrescine across pH 6.0-10.2.

    • Conclusions:

    • Human epidermis possesses transamidase activity.
    • The characterized epidermal transamidase shares functional similarities with other known transamidases, including fibrin cross-linking ability.