cDNA Cloning and Functional Expression of the α-d-Galactose-Binding Lectin Frutalin in Escherichia coli
作者： Carla Oliveira , Sofia Costa , José A. Teixeira , Lucília Domingues
DOI: 10.1007/S12033-009-9191-7
关键词:
摘要: cDNA clones encoding frutalin, the α-d-galactose-binding lectin expressed in breadfruit seeds (Artocarpus incisa), were isolated and sequenced. The deduced amino acid sequences indicated that frutalin may be encoded by a family of genes. NCBI database searches revealed sequence is highly homologous with jacalin mornigaG sequences. Frutalin was re-amplified cloned into commercial expression vector pET-25b(+) for production Escherichia coli. An experimental factorial design employed to maximise soluble recombinant lectin. results temperature, time induction, concentration IPTG interaction between induction had most significant effects on level frutalin. optimal culture conditions as follows: 1 mM at 22°C 20 h, yielding 16 mg/l SDS-PAGE Western blot analysis successfully bacteria expected molecular weight (17 kDa). These analyses also showed mainly produced insoluble protein. Recombinant agglutination properties carbohydrate-binding specificity similar native
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