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Human cathepsin D.

A J Barrett

    Advances in Experimental Medicine and Biology
    |January 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    This study details the purification and characterization of human liver Cathepsin D, a key enzyme involved in protein degradation. Researchers found it

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Molecular Biology

    Background:

    • Cathepsin D is a crucial aspartic protease involved in protein degradation.
    • Understanding its properties is vital for research into tissue damage and cellular processes.

    Purpose of the Study:

    • To purify and characterize human liver Cathepsin D.
    • To investigate its molecular properties, inhibition by pepstatin, and immunological characteristics.

    Main Methods:

    • Purification using autolysis, acetone fractionation, ion-exchange, and organomercurial-sepharose chromatography.
    • Separation of enzyme forms by preparative isoelectric focusing.
    • Characterization via molecular weight determination, amino acid analysis, and glycoprotein identification.

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    Main Results:

    • Human liver Cathepsin D (MW 43,000) was purified and identified as a glycoprotein.
    • Antisera demonstrated immunoinhibition of enzyme activity and localization in tissue damage.
    • Pepstatin inhibition revealed a pH-dependent conformational change affecting substrate binding.

    Conclusions:

    • Cathepsin D exists in multiple forms and is a glycoprotein.
    • Immunological methods can probe its function in cellular protein degradation.
    • Pepstatin is a potent inhibitor, with binding sensitive to pH-induced conformational changes.