Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum.

@article{BarrancoMedina2007BiochemicalAM,
  title={Biochemical and molecular characterization of the mitochondrial peroxiredoxin PsPrxII F from Pisum sativum.},
  author={Sergio Barranco-Medina and Tino Krell and Iris Finkemeier and Francisca Sevilla and Juan-Jos{\'e} L{\'a}zaro and K A Dietz},
  journal={Plant physiology and biochemistry : PPB},
  year={2007},
  volume={45 10-11},
  pages={729-39}
}
The pea peroxiredoxin homologue PsPrxII F of the Arabidopsis thaliana mitochondrial AtPrxII F was isolated as cDNA and genomic DNA, and characterized in respect to its biochemical and molecular properties. The deduced amino acid sequence contains an N-terminal targeting address for mitochondrial import. Mitochondrial location of PsPrxII F was confirmed by immunocytochemistry. The mature enzyme, without the transit peptide, has a molecular mass of 18.75 kDa, and, at positions 59 and 84, carries… CONTINUE READING
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