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Updated: Sep 30, 2026
Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
Published on: August 1, 2016
Expression and purification of the recombinant ConBr (Canavalia brasiliensis lectin) produced in Escherichia coli
Nadia A P Nogueira1, Moema B Grangeiro, Rodrigo M S da Cunha
1Depto. de Analises Clínicas e Toxicológicas, Universidade Federal do Ceara, Ceara, Brasil.
Abstract:
ConBr, a D-glucose/D-mannose-specific lectin from Canavalia brasiliensis seeds, was produced in Escherichia coli from a (c)DNA 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.
