Chemical synthesis and expression in E. coli of a human Val8-calcitonin gene by fusion to a synthetic human interferon-gamma gene.
A gene coding for human Val8-calcitonin (Val8-hCT) was synthesized by the solid-phase phosphite approach and fused to a synthetic human immune interferon-gamma (IFN-gamma) gene. The IFN gene was previously shown to be expressed at a very high level in E. coli [(1986) Gene, in press] due to the control of a strong synthetic promoter and strong ribosome binding site. The cells harboring the fused gene produced 100-150 micrograms per l of bacterial suspension of immunoreactive calcitonin in the form of hybrid IFN-gamma-Val8-hCT protein consisting of 140 amino acids. The Val8-hCT can be released from this protein by CNBr treatment.
D000595:Amino Acid Sequence; D001483:Base Sequence; D002116:Calcitonin / Q000031:analogs & derivatives* / Q000235:genetics; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis; D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D005813:Genes, Synthetic; D005822:Genetic Vectors; D006801:Humans; D007371:Interferon-gamma / Q000235:genetics*; D009693:Nucleic Acid Hybridization; D014158:Transcription, Genetic
D007371:Interferon-gamma; C050937:calcitonin, human, Val(8)-; D002116:Calcitonin; D004247:DNA