A relation between pyridine nucleotide-dependent dehydrogenase activity and nicotinamide adenine dinucleotide glycohydrolase in Ehrlich ascites tumor cells.

@article{Green1970ARB,
  title={A relation between pyridine nucleotide-dependent dehydrogenase activity and nicotinamide adenine dinucleotide glycohydrolase in Ehrlich ascites tumor cells.},
  author={Saul Green and A Dobrjansky},
  journal={Cancer research},
  year={1970},
  volume={30 2},
  pages={346-51}
}
The crystalline form of the glycolytic enzyme G3PDH2 from rabbit muscle may contain up to 4 moles NAD+/mole enzyme protein (29) and requires this NAD@ for the stabii zation of its structure and for protection against proteolytic inactivation by trypsin (1 1, 36). We have previously shown that the rate at which G3PDH-bound NAD@ was hydrolyzed was 20% that of the rate of hydrolysis of unbound NAD@ and that, as the bound NAD@ was hydrolyzed, the enzyme became increasingly susceptible to… CONTINUE READING
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