Kinetics and Equilibrium of the Inactivation of Ornithine Transcarbamylases by Pyridoxal Y-Phosphate *

@inproceedings{Margaret2002KineticsAE,
  title={Kinetics and Equilibrium of the Inactivation of Ornithine Transcarbamylases by Pyridoxal Y-Phosphate *},
  author={Margaret and Marshall and Philip P. Cohen},
  year={2002}
}
A phosphopyridoxyl derivative of bovine ornithine transcarbamylase (a trimer) prepared from an equimolar mixture of enzyme subunit and pyridoxal-P has been separated into homogeneous fractions (I to III) containing, respectively, one, two, and three phosphopyridoxyllysines per molecule, each on a different subunit. Fractions I and II have K,,,““’ unchanged and V ,,,aX proportional to the number of unmodified subunits remaining. Fraction III has K,“‘” increased 600-fold and is, therefore… CONTINUE READING