Abstract
Poly(ADP-ribose) catabolism is a complex situation involving many proteins and DNA. We have developed anin vitro turnover system where poly(ADP-ribose) metabolism is monitored in presence of different relative amounts of two principal enzymes poly(ADP-ribose) transferase and poly(ADP-ribose) glycohydrolase along with other proteins and DNA. Our current results reviewed here show that the quality of polymer, i.e. chain length and complexity, as well as preference for the nuclear substrate varies depending upon the availability of poly(ADP-ribose) glycohydrolase. These results are interpreted in the light of the recent data implicating poly(ADP-ribose) metabolism in DNA-repair. (Mol Cell Biochem 138: 45–52 1994)
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Lagueux, J., Shah, G.M., Ménard, L. et al. Poly(ADP-ribose) catabolism in mammalian cells. Mol Cell Biochem 138, 45–52 (1994). https://doi.org/10.1007/BF00928442
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DOI: https://doi.org/10.1007/BF00928442