【摘要】 利用PCR技术将透明颤菌血红蛋白基因(vgb)克隆到融合表达载体pET28a,在大肠杆菌BL21(DE3)表达。重组蛋白分别在30℃和37℃诱导表达,30℃诱导获得可溶性表达。结果表明:在30℃,1.5mmol/L和2.5mmol/LIPTG诱导下,诱导4～8h透明颤菌血红蛋白可获得高表达透明颤菌血红蛋白的表达量分别占菌体总蛋白的18.7%和27.7%。更多还原

【Abstract】 The vgb gene was cloned to the soluble expression vector PET28a,was expressed in E.coli BL21.The reconstructive protein was induced at 30 ℃and 37℃,respectively. The soluble expression was obtained at 30 ℃.The result showed: the vgb obtained high expression by induced four to eight hours at 30℃,using 1.5 mmol/L or 2.5 mmol/L IPTG-the expression products of veb accounted 18.7% and 27.7% at all protein.更多还原