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

[ Vol. 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   Pages 59 - 66 ( 8 )

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

Affiliation:

Depto. de Analises Clinicas e Toxicologicas, Universidade Federal do Ceara (UFC), Brasil



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