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Related Experiment Videos

Bovine thymus poly(adenosine diphosphate ribose) polymerase.

K Yoshihara, T Hashida, Y Tanaka

    The Journal of Biological Chemistry
    |September 25, 1978
    PubMed
    Summary
    This summary is machine-generated.

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    Researchers purified poly(adenosine diphosphate ribose) polymerase (PARP) from bovine thymus, finding it requires DNA for activation. Histones are not essential, but mask inhibitory DNA contaminants, suggesting PARP binds specific DNA sites.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Poly(adenosine diphosphate ribose) polymerase (PARP) is a crucial enzyme involved in DNA repair and other cellular processes.
    • Understanding PARP's activity and regulation is vital for comprehending DNA damage response pathways.

    Purpose of the Study:

    • To purify and characterize poly(adenosine diphosphate ribose) polymerase (PARP) from bovine thymus.
    • To investigate the essential factors and regulatory mechanisms for PARP enzyme activity.

    Main Methods:

    • Purification of PARP from bovine thymus extract using biochemical techniques.
    • Enzyme activity assays to determine cofactor requirements and kinetic parameters.
    • Analysis of enzyme composition and molecular weight.

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    Main Results:

    • Achieved a 1,300-fold purification of PARP with 10-20% recovery, yielding a 99% pure enzyme.
    • The purified PARP is a single 130,000 molecular weight peptide requiring NAD+, Mg2+, thiol, and DNA for activity.
    • Histones were found to mask inhibitory effects of denatured DNA, not essential for activation, and PARP appears to bind specific DNA sites.

    Conclusions:

    • The study successfully purified and characterized bovine thymus PARP.
    • PARP activation is DNA-dependent, with evidence suggesting specific DNA binding sites are involved in its regulation.
    • Histones play a modulatory role by mitigating inhibition from DNA contaminants.