Chemical synthesis and expression in E. coli of a human Val8‐ calcitonin gene by fusion to a synthetic human interferon‐γ gene

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Abstract
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‐γ (IFN‐γ) 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 μg per 1 of bacterial suspension of immunoreactive calcitonin in the form of hybrid IFN‐γ‐Val8‐hCT protein consisting of 140 amino acids. The Val8‐hCT can be released from this protein by CNBr treatment.