Glutamic dehydrogenase. I. The effect of coenzyme on the sedimentation velocity and kinetic behavior.

@article{Frieden1959GlutamicDI,
  title={Glutamic dehydrogenase. I. The effect of coenzyme on the sedimentation velocity and kinetic behavior.},
  author={Carl Frieden},
  journal={The Journal of biological chemistry},
  year={1959},
  volume={234 4},
  pages={809-14}
}
  • Carl Frieden
  • Published 1959 in The Journal of biological chemistry
It has been reported that high concentrations of reduced diphosphopyridine nucleotide as well as l,lO(ortho)-phenanthroline will cause dissociation of crystalline beef liver glutamic dehydrogenase as observed by the sedimentation behavior of the enzyme in the ultracentrifuge (1). Although this enzyme undergoes dissociation upon dilution (2), the effect of DPNH or l,lO-phenanthroline may be obtained at enzyme concentrations at which there should be essentially no dissociation at all. This result… CONTINUE READING