Lignin peroxidase from Phanerochaete chrysosporium. Molecular and kinetic characterization of isozymes.

@article{Glumoff1990LigninPF,
  title={Lignin peroxidase from Phanerochaete chrysosporium. Molecular and kinetic characterization of isozymes.},
  author={Tuomo Glumoff and Patricia J. Harvey and Susanna Molinari and Michele L Goble and Gerhard Frank and Joseph Michael Palmer and Jan Derk G. Smit and Matti S. A. Leisola},
  journal={European journal of biochemistry},
  year={1990},
  volume={187 3},
  pages={515-20}
}
Five isozymes of lignin peroxidase from Phanerochaete chrysosporium were purified and their physical, molecular and kinetic properties determined. The isozymes differ from each other in terms of their isoelectric point, molecular mass, sugar content, spectral characteristics, substrate specificity and stability. The N-terminal sequence of amino acids was different for each isozyme suggesting they are different gene products. The isozyme with the highest carbohydrate level was most sensitive to… CONTINUE READING

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