Inhibition by two lavendustins of the tyrosine kinase activity of pp60F527 in vitro and in intact cells.

@article{Agbotounou1994InhibitionBT,
  title={Inhibition by two lavendustins of the tyrosine kinase activity of pp60F527 in vitro and in intact cells.},
  author={W K Agbotounou and Kazuo Umezawa and Alain G Jacquemin-Sablon and Josiane Pierre},
  journal={European journal of pharmacology},
  year={1994},
  volume={269 1},
  pages={
          1-8
        }
}
The mutant pp60F527 protein possesses an activated protein-tyrosine kinase (PTK) activity correlated with a transforming activity. We have studied the inhibition of the pp60F527 PTK activity by two EGF-R tyrosine kinase inhibitors, lavendustin A and one of its derivatives, lavendustin C6. In vitro, both molecules were non-competitive inhibitors for the ATP binding site and uncompetitive inhibitors for the peptide binding site. The determined IC50S of the inhibition of pp60F527 kinase activity… CONTINUE READING

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