Kinetic and equilibrium studies on the activation of Escherichia coli K12 tryptophanase by pyridoxal 5'-phosphate and monovalent cations.

@article{HgbergRaibaud1975KineticAE,
  title={Kinetic and equilibrium studies on the activation of Escherichia coli K12 tryptophanase by pyridoxal 5'-phosphate and monovalent cations.},
  author={A H{\"o}gberg-Raibaud and Olivier Raibaud and Michel E. Goldberg},
  journal={The Journal of biological chemistry},
  year={1975},
  volume={250 9},
  pages={3352-8}
}
An improved purification of Escherichia coli K12 tryptophanase is presented. It is shown that the apoenzyme crystals, oxidized by exposure to air, can be reactivated by treatment with a reducing agent. The titration of sulfhydryl groups shows that four --SH groups are exposed and two are masked per protomer. The influence of two effectors, monovalent… CONTINUE READING