Inactivation of purified human recombinant monoamine oxidases A and B by rasagiline and its analogues.

@article{Hublek2004InactivationOP,
  title={Inactivation of purified human recombinant monoamine oxidases A and B by rasagiline and its analogues.},
  author={Frantisĕk Hub{\'a}lek and Claudia Binda and Min Li and Yaacov Herzig and Jeffrey E. Sterling and Moussa B. H. Youdim and Andrea Mattevi and Dale E. Edmondson},
  journal={Journal of medicinal chemistry},
  year={2004},
  volume={47 7},
  pages={1760-6}
}
The inactivation of purified human recombinant monoamine oxidases (MAO) A and B by rasagiline [N-propargyl-1(R)-aminoindan] and four of its analogues [N-propargyl-1(S)-aminoindan (S-PAI), 6-hydroxy-N-propargyl-1(R)-aminoindan (R-HPAI), N-methyl-N-propargyl-1(R)-aminoindan (R-MPAI), and 6-(N-methyl-N-ethyl carbamoyloxy)-N-propargyl-1(R)-aminoindan (R-CPAI)] has been investigated. All compounds tested, with the exception of R-CPAI, form stoichiometric N(5) flavocyanine adducts with the FAD moiety… CONTINUE READING