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. 2002 Feb;9(1):59-66.
doi: 10.2174/0929866023408968.

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

Nadia A P Nogueira  1 , 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
Affiliations

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

Nadia A P Nogueira et al. Protein Pept Lett. 2002 Feb.

Abstract

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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