Affinity purification and characterization of 2,4-dichlorophenol hydroxylase from Pseudomonas cepacia.

@article{Radjendirane1991AffinityPA,
  title={Affinity purification and characterization of 2,4-dichlorophenol hydroxylase from Pseudomonas cepacia.},
  author={V Radjendirane and Muzafer A. Bhat and Chelakard S. Vaidyanathan},
  journal={Archives of biochemistry and biophysics},
  year={1991},
  volume={288 1},
  pages={169-76}
}
2,4-Dichlorophenol hydroxylase, a flavoprotein monooxygenase from Pseudomonas cepacia grown on 2,4-dichlorophenoxyacetic acid (2,4-D) as the sole source of carbon, was purified to homogeneity by a single-step affinity chromatography on 2,4-DCP-Sepharose CL-4B. The enzyme was eluted from the affinity matrix with the substrate 2,4-dichlorophenol. The enzyme has a molecular weight of 275,000 consisting of four identical subunits of molecular weight 69,000 and requires exogenous addition of FAD for… CONTINUE READING

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