Multiple joined genes prevent product degradation in Escherichia coli

摘要: Abstract A method is described that allows the expression of a stable human proinsulin product in Escherichia coli as encoded by either fused or an unfused gene construction. In system, coding sequence joined to 3' side fragment containing lac promoter and for small part NH2 terminus beta-galactosidase. linked directly Tac followed bacterial Shine-Dalgarno sequence. both systems, too unstable be detected NaDodSO4/polyacrylamide gel electrophoresis even pulse-chase analysis. However, when multiple copies are tandemly such resultant protein contains domain, stability markedly increased systems. three polypeptide domains required stabilization, whereas two plus leader enhance system. The copy can cleaved into single units cyanogen bromide treatment.