DOI: 10.1111/j.1432-1033.1984.tb08314.x. Poly(ADP‐ribose) polymerase is a zinc metalloenzyme

Poly(ADP‐ribose) polymerase is a zinc metalloenzyme

10.1111/j.1432-1033.1984.tb08314.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

Purified poly(ADP‐ribose) polymerase was inhibited by 1,10‐phenanthroline at pH <8. This inhibition and the inhibition by other chelating agents suggested that this enzyme was a metalloprotein. Atomic absorption spectroscopy showed the presence of one atom of zinc per protein molecule. Dialysis of the enzyme against buffers containing 1,10‐phenanthroline resulted in the loss of activity and the removal of zinc from the enzyme. Initial rate kinetics snowed that 1,10‐phenanthroline was non‐competitive with NAD+ and competitive with DNA. The binding of DNA to the enzyme was unaffected by the inhibitor. These results suggest that a metal‐containing site is involved as part of the interaction of DNA and poly(ADP‐ribose) polymerase.

Bibliography

ZAHRADKA, P., & EBISUZAKI, K. (1984). Poly(ADPâribose) polymerase is a zinc metalloenzyme. European Journal of Biochemistry, 142(3), 503â509. Portico.

Authors 2

Peter ZAHRADKA (first)
Kaney EBISUZAKI (additional)

References 58 Referenced 100

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Dates

Type	When
Created	20 years, 6 months ago (March 3, 2005, 6:12 p.m.)
Deposited	1 year, 9 months ago (Nov. 23, 2023, 5:30 p.m.)
Indexed	47 minutes ago (Sept. 4, 2025, 5:08 a.m.)
Issued	41 years, 1 month ago (Aug. 1, 1984)
Published	41 years, 1 month ago (Aug. 1, 1984)
Published Online	20 years, 6 months ago (March 3, 2005)
Published Print	41 years, 1 month ago (Aug. 1, 1984)

Funders 0

None

BibTeX

@article{ZAHRADKA_1984, title={Poly(ADP‐ribose) polymerase is a zinc metalloenzyme}, volume={142}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1984.tb08314.x}, DOI={10.1111/j.1432-1033.1984.tb08314.x}, number={3}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={ZAHRADKA, Peter and EBISUZAKI, Kaney}, year={1984}, month=aug, pages={503–509} }

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