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Related Experiment Videos

Poly(ADP-ribosylation) in Ascaris suum.

R D Walter, E Ossikovski

    Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
    |July 1, 1984
    PubMed
    Summary

    Poly(ADP-ribosylation) activity was found in the Ascaris suum parasite, particularly in reproductive tissues. This enzyme activity is dependent on divalent cations and inhibited by various compounds like nicotinamide.

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    Area of Science:

    • Biochemistry
    • Parasitology
    • Molecular Biology

    Background:

    • Poly(ADP-ribosylation) is a post-translational modification crucial in DNA repair and other cellular processes.
    • The presence and characteristics of poly(ADP-ribosylation) enzymes in parasitic organisms like Ascaris suum are not well-understood.

    Purpose of the Study:

    • To investigate the presence and characterize the activity of poly(ADP-ribosylation) in the intestinal parasite Ascaris suum.
    • To determine the optimal conditions and kinetic properties of the ADP-ribosyltransferase enzyme in Ascaris suum.

    Main Methods:

    • Enzyme assays were performed to detect and quantify poly(ADP-ribosylation) activity.
    • The effects of divalent cations, deoxyribonuclease I, temperature, and pH on enzyme activity were assessed.
    • Kinetic parameters (Km) and inhibition constants (Ki) were determined using various inhibitors.

    Main Results:

    • Poly(ADP-ribosylation) activity was confirmed in Ascaris suum, with higher levels in reproductive tissues.
    • Enzyme activity was dependent on divalent cations and significantly stimulated by deoxyribonuclease I.
    • Optimal activity was observed at 30°C and pH 8.4, with an apparent Km for NAD of 0.2mM.
    • Nicotinamide, benzamide, 3-aminobenzamide, theophylline, and thymidine competitively inhibited the enzyme with respect to NAD.

    Conclusions:

    • A functional poly(ADP-ribosylation) system exists in Ascaris suum, predominantly in reproductive tissues.
    • The characterized ADP-ribosyltransferase exhibits properties similar to those found in other organisms, suggesting conserved mechanisms.
    • The identified inhibitors provide potential targets for further research into parasitic biochemical pathways.

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