Kinetic and electrophoretic properties of native and recombined isoenzymes of human liver alcohol dehydrogenase.

@article{Bosron1983KineticAE,
  title={Kinetic and electrophoretic properties of native and recombined isoenzymes of human liver alcohol dehydrogenase.},
  author={William F. Bosron and Leslie J. Magnes and T. K. Li},
  journal={Biochemistry},
  year={1983},
  volume={22 8},
  pages={1852-7}
}
Ten, electrophoretically distinct, molecular forms of alcohol dehydrogenase have been isolated from a single human liver by affinity and ion-exchange chromatography. The starch gel electrophoresis patterns after the dissociation-recombination of the forms are consistent with the hypothesis that they arise from the random combination of alpha, beta 1, gamma 1, and gamma 2 subunits into six heterodimeric and four homodimeric isoenzymes. Large differences in kinetic properties are observed for the… CONTINUE READING

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