• Chemistry, Medicine
  • Published in
    The Journal of biological…
    1966

A reinterpretation of the stabilization of tryptophan pyrrolase by its substrate.

@article{Knox1966ARO,
  title={A reinterpretation of the stabilization of tryptophan pyrrolase by its substrate.},
  author={William E. Knox and Marta M. Piras},
  journal={The Journal of biological chemistry},
  year={1966},
  volume={241 3},
  pages={
          764-7
        }
}
Abstract The loss of activity of the liver tryptophan pyrrolase when it is incubated without tryptophan can be reversed. Crude tryptophan pyrrolase preparations, in general, are slowly activated by incubation with tryptophan, methemoglobin, and ascorbate, during which conjugation of the apoenzyme and its reduction to the active, reduced holoenzyme occurs. Aerobic incubation without tryptophan inactivates without unconjugating the enzyme, apparently by forming the reversibly inactivated… CONTINUE READING

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