Purification and some properties of two isofunctional juglone hydroxylases from Pseudomonas putida J1.

Abstract

Juglone-induced cells of Pseudomonas putida J 1 were shown to contain two isofunctional juglone hydroxylases. Both enzymes were purified about 125-fold to homogeneity in polyacrylamide gel electrophoresis. The molecular masses of the native enzymes, as determined by Sephacryl S-200 gel filtration were 59 000 Da for enzyme 1 and 56 000 Da for enzyme 2. The… (More)

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@article{Rettenmaier1985PurificationAS, title={Purification and some properties of two isofunctional juglone hydroxylases from Pseudomonas putida J1.}, author={Heinz Rettenmaier and Franz Lingens}, journal={Biological chemistry Hoppe-Seyler}, year={1985}, volume={366 7}, pages={637-46} }