Kinetic behaviour of soluble and mitochondrial bound lactate dehydrogenase.

@article{Sanz1990KineticBO,
  title={Kinetic behaviour of soluble and mitochondrial bound lactate dehydrogenase.},
  author={M. C. {\'A}lvarez Sanz and M. Luisa Sagrist{\'a} and Carmen Lluis},
  journal={The Italian journal of biochemistry},
  year={1990},
  volume={39 1},
  pages={21-9}
}
Rabbit liver mitochondrial fraction shows lactate dehydrogenase activity. The kinetic behaviour of mitochondrial bound enzyme fits a bibi sequential type mechanism as well as the cytosolic rabbit liver lactate dehydrogenase. The bound enzyme has greater values of Km(NADH) and Km(pyruvate) than the soluble one, suggesting that binding induces a decrease in the affinity of both substrates. The behaviour of the free and the mitochondrial-bound enzyme is of the Michaelis-Menten type, but the… CONTINUE READING

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