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Cathepsin B from human renal cortex

A D Gounaris, E E Slater

    The Biochemical Journal
    |August 1, 1982
    PubMed
    Summary
    This summary is machine-generated.

    Researchers identified cysteine-proteinase activity in human kidney tissue, purifying the enzyme and identifying it primarily as cathepsin B. This finding advances our understanding of renal enzymes.

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    Area of Science:

    • Biochemistry
    • Renal Physiology
    • Enzymology

    Background:

    • Cysteine-proteinase activity exists in human renal cortex homogenates.
    • This activity is initially associated with renin enzymic activity.

    Purpose of the Study:

    • To purify and characterize cysteine-proteinase from human cadaver renal cortex.
    • To identify the specific type(s) of cysteine-proteinase present.

    Main Methods:

    • Purification involved sequential chromatography: Sephadex G-75, DEAE-cellulose DE-52, and organomercurial affinity resin.
    • Enzyme characterization included pH dependence, stability, substrate specificity, and molecular size determination.
    • Activity assays utilized synthetic substrates like alpha-N-benzoyl-DL-arginine 2-naphthylamide (Bz-Arg-NNap).

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    Main Results:

    • A cysteine proteinase was purified 1780-fold.
    • The major component (95%) was identified as cathepsin B (26,000 daltons).
    • A minor component (5%) showed characteristics suggestive of cathepsin H.

    Conclusions:

    • The primary cysteine-proteinase in human renal cortex is cathepsin B.
    • The study provides a detailed characterization of this renal enzyme.
    • Methodological considerations for substrate preparation were highlighted.