Ivanov I, Gigova L, Jay E
FEBS Lett. 1987 Jan 1;210(1):56-60. doi: 10.1016/0014-5793(87)81297-8.
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.
通过固相亚磷酸酯法合成了编码人Val8 - 降钙素（Val8 - hCT）的基因，并将其与合成的人免疫干扰素 - γ（IFN - γ）基因融合。由于受强合成启动子和强核糖体结合位点的控制，该IFN基因先前已被证明在大肠杆菌中能以非常高的水平表达[（1986年）《基因》，待发表]。携带融合基因的细胞每升细菌悬液产生100 - 150微克具有免疫反应性的降钙素，其形式为包含140个氨基酸的杂合IFN - γ - Val8 - hCT蛋白。通过溴化氰处理可从该蛋白中释放出Val8 - hCT。
