Purification and specific kinetic properties of erythrocyte uridine diphosphate glucose pyrophosphorylase.

@article{Tsuboi1969PurificationAS,
  title={Purification and specific kinetic properties of erythrocyte uridine diphosphate glucose pyrophosphorylase.},
  author={Kenneth K. Tsuboi and Kohji Fukunaga and John C. Petricciani},
  journal={The Journal of biological chemistry},
  year={1969},
  volume={244 3},
  pages={
          1008-15
        }
}
The enzyme uridine diphosphate glucose pyrophosphorylase has been prepared at high purity (specific activity 127) from the human erythrocyte. Comparison of its specific properties with enzyme isolated from liver indicates many similarities including size. Examination of the reversible reaction catalyzed by the erythrocyte enzyme from both forward and reverse directions revealed a highly selective product inhibition by UDP-glucose. Since a dual enzyme function involving both regulation and… CONTINUE READING
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