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Related Experiment Videos

Protein factor which induces conversion between Physarum ornithine decarboxylase forms in vitro

J L Mitchell, T A Augustine, J M Wilson

    Biochimica Et Biophysica Acta
    |January 15, 1981
    PubMed
    Summary

    Researchers isolated a novel protein factor regulating ornithine decarboxylase activity in Physarum polycephalum. This factor catalyzes the conversion of the active enzyme to a less active form, crucial for enzyme regulation.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Ornithine decarboxylase (ODC) activity is rapidly modulated in Physarum polycephalum.
    • This modulation is linked to reversible post-translational modifications of the enzyme.

    Purpose of the Study:

    • To isolate and characterize a factor responsible for ODC activity modulation.
    • To investigate the mechanism of ODC interconversion between active and inactive states.

    Main Methods:

    • Isolation of the A-B converting factor from microplasmodia homogenates.
    • Purification using DEAE-Sephacel chromatography and Ultrogel AcA-34 gel filtration.
    • Characterization of the factor's properties (heat lability, acidity, molecular weight).

    Main Results:

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    • A heat-labile, acidic protein factor (approx. 35,000 MW) was isolated.
    • The factor catalyzes the conversion of active ODC (A) to a less active form (B).
    • Conversion requires spermidine or spermine and is inhibited by chelators like ATP, ADP, and GTP.

    Conclusions:

    • This study reports the first isolation of a protein factor involved in ODC interconversion.
    • The factor's activity is dependent on polyamines and ionic strength.
    • The interaction appears stoichiometric and irreversible under tested conditions.