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: http://dx.doi.org/10.2174/0929866023408968

Publication date: 2002-02-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.