Evidence for the existence of discrete activator and substrate sites for CO2 on ribulose-1,5-bisphosphate carboxylase.

@article{Lorimer1979EvidenceFT,
  title={Evidence for the existence of discrete activator and substrate sites for CO2 on ribulose-1,5-bisphosphate carboxylase.},
  author={George H Lorimer},
  journal={The Journal of biological chemistry},
  year={1979},
  volume={254 13},
  pages={5599-601}
}
When incubated with CO2 and Mg2+, ribulose-1,5-bis-phosphate carboxylase forms a ternary complex of enzyme . CO2 . Mg. This complex was prepared using high specific activity [14C]O2 and injected into a solution containing a large (50- to 112-fold) molar excess of [12C]O2 and sufficient ribulose 1,5-bisphosphate to permit the catalytic site to turn over several times. The enzyme was then rapidly separated from the other components by gel filtration and its radiospecific activity was determined… CONTINUE READING