低氧诱导透明颤菌血红蛋白基因在大肠杆菌中的表达

Hypoxia-induced Expression of Vitreoscilla Hemoglobin Gene in Escherichia coli

合成透明颤菌血红蛋白基因(vgb)的天然低氧启动子,与vgb结构基因拼接得到570 bp的vgb基因,将该基因克隆到pUC18质粒中重组为pUC_LV质粒,转化大肠杆菌得到重组子。通过低氧诱导10 h后,重组菌的密度较对照增加了67.4%,经SDS_PAGE和CO差光谱分析证明重组菌表达了有活性的透明颤菌血红蛋白(VHb)。

The 570 bp Vitreoscilla hemoglobin gene （ vgb ） was obtained by synthesizing the native promoter of vgb and jointing it with vgb structural gene. The recombinant vector pUC-LV constructed by cloning the gene into pUC18 plasmid was transformed into Escherichia coli. After ten hours of induction under low dissolved oxygen conditions, the density of recombinant strain increased 67.4% compaired with that of control. The results of SDS-PAGE and carbon monoxide（CO） difference spectrum analysis indicated that the recombinant strain expressed Vitreoscilla hemoglobin （VHb） having biological activity.