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Cathepsins D from rhesus monkey lung. Purification and characterization

A Moriyama, K Takahashi

    Journal of Biochemistry
    |September 1, 1980
    PubMed
    Summary

    Two cathepsin D proteases were purified from rhesus monkey lung. Cathepsin D-II exhibited remarkable stability across a wide pH range, suggesting broader functional capabilities in vivo.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Primate Biology

    Background:

    • Cathepsin D is a key aspartic protease involved in protein degradation.
    • Understanding cathepsin D function in non-human primates is crucial for comparative biology and disease modeling.

    Purpose of the Study:

    • To purify and characterize two distinct forms of cathepsin D from rhesus monkey lung.
    • To compare the enzymatic properties and stability of these cathepsin D variants.

    Main Methods:

    • Purification of cathepsin D-I and D-II using techniques like disc gel electrophoresis.
    • Determination of molecular weight via Sephadex G-100 chromatography and SDS-PAGE.
    • Enzyme activity assays using hemoglobin, albumin, and insulin B-chain at various pH levels.
    • Stability assays across a range of pH conditions.
    • Inhibition studies using specific acid protease inhibitors.

    Main Results:

    • Two homogeneous cathepsin D forms (D-I and D-II) were isolated with differential yields.
    • Both cathepsins D had a molecular weight of approximately 35,000-41,000 Da.
    • Cathepsin D-I showed optimal activity at acidic pH (3.4-4.0) and was pH-sensitive, while Cathepsin D-II demonstrated exceptional stability from pH 1-9.
    • Both proteases hydrolyzed various peptide bonds in insulin B-chain and hemoglobin, with Cathepsin D-II showing broader substrate cleavage at different pH.
    • Both enzymes were inhibited by acid protease inhibitors, with Cathepsin D-II being less susceptible to most.

    Conclusions:

    • Rhesus monkey lung contains at least two distinct cathepsin D proteases with differing biochemical properties.
    • Cathepsin D-II's remarkable pH stability suggests a significant role in diverse physiological and pathological conditions within the lung.
    • These findings provide insights into the functional diversity of cathepsin D in primates.

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