Expression and purification of the recombinant ConBr (Canavalia brasiliensis lectin) produced in Escherichia coli cells.

نویسندگان

  • Nadia A P Nogueira
  • Moema B Grangeiro
  • Rodrigo M S da Cunha
  • Marcio V Ramos
  • Maria A O Alves
  • Edson H Teixeira
  • Manoel Barral-Netto
  • Juan J Calvete
  • Benildo S Cavada
  • Thalles B Grangeiro
چکیده

ConBr, a D-glucose/D-mannose-specific lectin from Canavalia brasiliensis seeds, was produced in Escherichia coli from a (c)DNA clone subcloned to pET15b expression vector. The recombinant lectin (rConBr) was purified by one-step immobilized metal-affinity chromatography using an amino-terminal hexahistidine tag. By SDS-PAGE and Western blot, rConBr was highly pure with an apparent molecular mass of 37 kDa. N-terminal sequence analysis revealed a single sequence, confirming the identity of the expressed protein as the pre-pro-ConBr.

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عنوان ژورنال:
  • Protein and peptide letters

دوره 9 1  شماره 

صفحات  -

تاریخ انتشار 2002