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Arginase from human full-term placenta.

R Porta, C Esposito, A Martin

    The Biochemical Journal
    |December 1, 1976
    PubMed
    Summary
    This summary is machine-generated.

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    Human placenta arginase was purified and characterized. This metalloenzyme has a molecular weight of 70,000 and an optimal pH of 9.1, with specific inhibition patterns observed.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Human Physiology

    Background:

    • Arginase is a key enzyme in the urea cycle, catalyzing the hydrolysis of L-arginine to L-ornithine and urea.
    • Human placenta is a rich source of various enzymes, including arginase, which plays a role in amino acid metabolism during pregnancy.

    Purpose of the Study:

    • To purify and characterize arginase from human full-term placenta.
    • To determine the enzyme's molecular weight, optimal pH, and kinetic properties.

    Main Methods:

    • Purification of arginase using techniques such as disc electrophoresis and molecular-sieve chromatography.
    • Determination of molecular weight via gel filtration and SDS-PAGE.
    • Enzyme kinetics assays to determine optimal pH and Km for L-arginine.

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    Main Results:

    • Arginase was purified approximately 1800-fold, appearing homogenous.
    • The molecular weight was determined to be 70,000 Da.
    • The enzyme exhibited an optimal pH of 9.1 and a Km for L-arginine of 27 mM.
    • L-ornithine and L-lysine competitively inhibited the enzyme with Ki values of 6.3 mM and 14 mM, respectively.

    Conclusions:

    • Human placenta arginase is a metalloenzyme with specific kinetic and inhibition characteristics.
    • The purified enzyme provides a valuable tool for further biochemical and physiological studies.
    • Understanding arginase properties is crucial for metabolic research and potential therapeutic applications.