Expression and Purification of the Recombinant Conbr (Canavalia Brasiliensis Lectin) Produced in Escherichia Coli Cells

Title: Expression and Purification of the Recombinant Conbr (Canavalia Brasiliensis Lectin) Produced in Escherichia Coli Cells

Volume: 9 Issue: 1

Author(s): 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 and Thalles B. Grangeiro

Affiliation:

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

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.

Cite this article as:

Nogueira A.P. Nadia, Grangeiro B. Moema, da Cunha M.S. Rodrigo, Ramos V. Marcio, Alves A.O. Maria, Teixeira H. Edson, Barral-Netto Manoel, Calvete J. Juan, Cavada S. Benildo and Grangeiro B. Thalles, Expression and Purification of the Recombinant Conbr (Canavalia Brasiliensis Lectin) Produced in Escherichia Coli Cells, Protein & Peptide Letters 2002; 9 (1) . https://dx.doi.org/10.2174/0929866023408968