Phytoalexin synthesis in soybean: purification and reconstitution of cytochrome P450 3,9-dihydroxypterocarpan 6a-hydroxylase and separation from cytochrome P450 cinnamate 4-hydroxylase.

@article{Kochs1989PhytoalexinSI,
  title={Phytoalexin synthesis in soybean: purification and reconstitution of cytochrome P450 3,9-dihydroxypterocarpan 6a-hydroxylase and separation from cytochrome P450 cinnamate 4-hydroxylase.},
  author={Georg Kochs and Hans Grisebach},
  journal={Archives of biochemistry and biophysics},
  year={1989},
  volume={273 2},
  pages={543-53}
}
Elicitor-challenged soybean (Glycine max) cell cultures were used for detergent solubilization and purification of cytochrome P450 3,9-dihydroxypterocarpan 6a-hydroxylase (D6aH). D6aH was purified to electrophoretic homogeneity from such cells by a five-step procedure. It could be separated from cytochrome P450 cinnamate 4-hydroxylase on hydroxyapatite. This is the first report on separation of two cytochrome P450 enzymes from a higher plant. On sodium dodecyl sulfate polyacrylamide gels D6aH… CONTINUE READING

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