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

Authors: Nogueira N.A.P.; Grangeiro M.B.; da Cunha R.M.S.; Ramos M.V.; Alves M.A.O.; Teixeira E.H.; Barral-Netto M.; Calvete J.J.; Cavada B.S.; Grangeiro T.B.

Source: Protein and Peptide Letters, Volume 9, Number 1, February 2002 , pp. 59-66(8)

Publisher: Bentham Science Publishers

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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

Language: English

Document Type: Review article

DOI: 10.2174/0929866023408968

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