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已构建好的白细胞介素２－粒／巨噬细胞集落刺激因子（ＩＬ２－ＧＭＣＳＦ）融合基因载体，转化大肠杆菌ＤＨ５α，进行热诱导表达条件的研究。工程菌在３０℃培养活化至ＯＤ６００ｎｍ＝０．５±０．１时，融合蛋白的表达率最为稳定；而后转为４２℃热诱导４±０．５ｈ，蛋白表达效率最高。
The interleukin-2 / granulocyte-macrophage colony-stimulating factor (IL2-GMCSF) fusion gene vector has been constructed and transformed into Escherichia coli DH5α to study the conditions of heat-induced expression. When the engineered bacteria were cultured and activated at 30 ° C to OD600nm = 0.5 ± 0.1, the expression rate of the fusion protein was the most stable; then it was heat-induced at 42 ° C for 4 ± 0.5h and the protein expression efficiency was the highest.