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利用人工全合成人胰岛素样生长因子工（ｈＩＧＦ－Ｉ）基因，构建了分别以β－半乳糖苷醇（β－ｇａｌ）的三种即含５９０、３１０、２８０个氨基酸序列片段和一种以ＰｒｏｔｅｉｎＡ的Ｂ、Ｃ结构域（ＰＡＢＣ）为载体蛋白的融合型表达质粒，并在大肠杆菌中高效表达了以上各种ｈＩＧＦ－Ｉ的融合蛋白产物。通过对羟胺裂解前后的ｈＩＧＦ－Ｉ产物进行放射免疫结合测定分析，结果显示以β－Ｇａｌ６９０、３１０、２８０为载体蛋白，均严重影响与其融合的ｈＩＧＦ－Ｉ的免疫原性结构形成，但在ＰＡＢＣ－ｈＩＧＦ－Ｉ融合蛋白中，载体蛋白ＰＡＢＣ无明显的影响作用。这表明在高融合表达低分子量蛋白或肽段中，需选择适宜的载体蛋白，以利于目的产物的功能性结构形成。
Using artificial full-length human insulin-like growth factor (hIGF-I) gene, we constructed the three kinds of β-galactosidase (β-gal) containing 590,310,280 amino acid sequence fragments and a Protein A B, C domain (PABC) as a carrier protein fusion expression plasmid, and highly expressed in E. coli hIGF-I of the above fusion protein products. The results of radioimmunoassay analysis of hIGF-I products before and after hydroxylamine cleavage showed that the immunogenicity of hIGF-I fused with β-Gal690,310,280 as a carrier protein seriously affected the immunogenicity of the formation of hIGF-I. However, -hIGF-I fusion protein, carrier protein PABC no significant effect. This suggests that in high fusion expression of low molecular weight proteins or peptides, the need to select the appropriate carrier protein, in order to facilitate the formation of the functional structure of the desired product.