Kinetic equivalence of the active sites of alcohol dehydrogenase from horse liver.

@article{Hadorn1975KineticEO,
  title={Kinetic equivalence of the active sites of alcohol dehydrogenase from horse liver.},
  author={M Hadorn and Vivian A. John and Frederick Meier and H Dutler},
  journal={European journal of biochemistry},
  year={1975},
  volume={54 1},
  pages={65-73}
}
The reduction, catalysed by liver alcohol dehydrogenase, of benzaldehyde in the presence and absence of pyrazole, and the oxidation of benzyl alcohol and cyclohexanol in the presence of isobutyramide, has been measured by the stopped-flow technique. In performing these experiments particular care was taken to purify the enzyme, coenzymes, substrates and inhibitors, and to minimise as much as possible the effects of a blank substrate reaction. The calculation of the amount of substrate converted… CONTINUE READING