Reconstitution and poly(ADP-ribosyl)ation of proteolytically fragmented poly(ADP-ribose) synthetase.

@article{Kameshita1986ReconstitutionAP,
  title={Reconstitution and poly(ADP-ribosyl)ation of proteolytically fragmented poly(ADP-ribose) synthetase.},
  author={Isamu Kameshita and Masao Matsuda and Morimitsu Nishikimi and Hiroshi Ushiro and Yutaka Shizuta},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 8},
  pages={3863-8}
}
Calf thymus poly(ADP-ribose) synthetase (Mr = 120,000) is cleaved with papain into two fragments of M(r) = 74,000 and 46,000 and also split with chymotrypsin into two fragments of M(r) = 66,000 and 54,000. Each fragment purified to homogeneity is enzymatically inactive, but combined incubation of the 74,000 and 46,000 fragments in the presence of DNA restored 20% of the enzyme activity. In contrast, combined incubation of the 66,000 and 54,000 fragments does not restore any enzyme activity. In… CONTINUE READING