Phenylalanine hydroxylase from Chromobacterium violaceum. Purification and characterization.

@article{Nakata1979PhenylalanineHF,
  title={Phenylalanine hydroxylase from Chromobacterium violaceum. Purification and characterization.},
  author={Hiroyasu Nakata and Takashi Yamauchi and Hitoshi Fujisawa},
  journal={The Journal of biological chemistry},
  year={1979},
  volume={254 6},
  pages={1829-33}
}
Phenylalanine hydroxylase was purified approximately 3000-fold to apparent homogeneity with a 13% yield and crystalized from L-phenylalanine-induced cells of Chromobacterium violaceum. The enzyme was shown to be composed of a single polypeptide chain with an estimated molecular weight of approximately 32,000. Some of the physical properties of the enzyme include: a Stokes radius of 26.0 A, a sedimentation coefficient of 2.71 S, a diffusion coefficient of 8.20 X 10(-7) CM2/S, a frictional ratio… CONTINUE READING

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