Expression and purification of the recombinant ConBr (Canavalia brasiliensis lectin) produced in Escherichia coli cells
- Nogueira, Nadia A. P
- Grangeiro, Moema B
- Cunha, Rodrigo M. S. da
- Ramos, Marcio V
- Alves, Maria A. O
- Teixeira, Edson H
- Barral Netto, Manoel
- Calvete, Juan J
- Cavada, Benildo Sousa
- Grangeiro, Thalles B
Publication date
January 2002
DOI Publisher
Bentham Science Publishers Ltd. ISSN
0929-8665 Citation count (estimate)
5Abstract
ConBr, a D-glucose/D-mannose-specific lectin from Canavalia brasiliensis seeds, was produced in Escherichia coli from a cDNA clone subcloned to pET15b expression vector. The recombinant lectin (rConBr) was purified by onestep 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
Add to ORKG