Abstract
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 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.
Keywords: D-mannose-specific, amino-terminal, branched chain trimannoside, carbohydrate-binding site, horseradish peroxidase, anti-ConBr antibody
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