23 research outputs found
Spectrofluorodensitometric estimation in thin-layer chromatography of gibberellic acid produced by solid-state fermentation
Fed-Batch culture for the direct conversion of cellulosic substrates to acetic acid/ethanol by Fusarium oxysporum
Structure in the local environment of Zn<sup>2+</sup>ion in the anti-termination protein of<i>Bacillus subtilis</i>
Supercritical fluid extraction from dry mouldy bran for the purification of gibberellic acid from the concomitant products produced during solid state fermentation
Crystal structure of a decamer RNA r(ggcggucgcu)2 with terminal and tandem G{middle dot}U wobble base-pairs
Identification of phosphate oxygens that are important for self-cleavage activity of the HDV ribozyme by phosphorothioate substitution interference analysis
Expression of highly active recombinant NS3 protease domain of hepatitis C virus in E. coli
AbstractThe serine protease domain of HCV comprising amino acids 1027–1218 (ΔNS3) was expressed in E. coli with a His tag at its N-terminal end. The protease was purified to apparent homogeneity by a single step affinity chromatography resulting in high yields (∼3 mg/l of cultured cells). The ΔNS3 efficiently cleaves a 17-mer peptide corresponding to the NS5A-NS5B junction with kcat/Km=160×10−3 min−1 μM−1 in the presence of NS4A peptide. Our ΔNS3 represents the minimal domain possessing highly active protease of NS3 constructed so far. The ΔNS3 protein also efficiently processed a longer substrate corresponding to NS5A/5B junction (2203–2506 amino acids) that was synthesized by in vitro transcription and translation system
