Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies.

@article{Porcino2012LeishmaniaB,
  title={Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies.},
  author={Gabriane Nascimento Porcino and Cristiane de Carvalho-Campos and Ana Carolina Ribeiro Gomes Maia and Michelle de Lima Detoni and Priscila Faria-Pinto and Elaine Soares Coimbra and Marcos Jos{\'e} Marques and Maria Aparecida Juliano and Luiz Juliano and Vanessa {\'A}lvaro Diniz and Suzana C{\^o}rte-Real and Eveline Gomes Vasconcelos},
  journal={Experimental parasitology},
  year={2012},
  volume={132 2},
  pages={293-9}
}
Nucleoside triphosphate diphosphohydrolase (NTPDase) activity was recently characterized in Leishmania (Viannia) braziliensis promastigotes (Lb), and an antigenic conserved domain (r82-121) from the specific NTPDase 1 isoform was identified. In this work, mouse polyclonal antibodies produced against two synthetic peptides derived from this domain (LbB1LJ, r82-103; LbB2LJ, r102-121) were used. The anti-LbB1LJ or anti-LbB2LJ antibodies were immobilized on protein A-sepharose and… CONTINUE READING
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Immunostimulatory property of a synthetic peptide belonging to the soluble ATP diphosphohydrolase isoform (SmATPDase 2) and immunolocalisation of this protein in the Schistosoma mansoni

  • Mendes, R.G.P.R, +12 authors E. G. Vasconcelos
  • egg. Mem. Inst
  • 2011
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