Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin.

@article{Marchand2006ComparativePA,
  title={Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin.},
  author={Christophe H Marchand and Pierre Le Mar{\'e}chal and Yves Meyer and Paulette Decottignies},
  journal={Proteomics},
  year={2006},
  volume={6 24},
  pages={6528-37}
}
Thioredoxin (TRX) is a small multifunctional protein with a disulfide active site involved in redox regulation. To gain insight into the numerous proteins able to interact with thioredoxin in Arabidopsis thaliana, we have compared three different proteomic procedures. In the two first approaches targets present in a mixture of soluble leaf proteins were reduced by the cytosolic TRX h3, then the new thiols were labeled either with radioactive iodoacetamide allowing specific detection (first… CONTINUE READING

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