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

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, Thalles B. Grangeiro

Journal Name: Protein & Peptide Letters

Volume 9 , Issue 1 , 2002

Become EABM
Become Reviewer
Call for Editor


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

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2002
Published on: 01 March, 2012
Page: [59 - 66]
Pages: 8
DOI: 10.2174/0929866023408968

Article Metrics

PDF: 42