人防御素 hβD-3基因在大肠埃希菌中的融合表达

Fusion Expression of Human Defensin hβD-3 Gene in Escherichia coli

摘要: 研究了人类防御素hβD-3基因在大肠埃希菌细胞中的融合表达，采用pET-32a(+)载体在BL21(DE3)溶原菌中进行了F-βD-3蛋白的融合表达.结果表明，F-βD-3蛋白的表达量达到127.23 μg/mL，融合蛋白经镍柱亲和层析与肠激酶酶切后，最终得到hβD-3蛋白的量为18.17 μg/mL.经对大肠埃希菌K₁₂D₃₁ 的抑菌试验鉴定，肠激酶酶切后产物为有抑菌活性的重组hβD-3蛋白.

Abstract: The fusion expression strategy of human beta defensin 3(hβD-3) gene in Escherichia coli cells in the fusion expression by pET-32a(+) vector was studied. Fusion expression of F-βD-3 protein was performed in lysogenic bacterium BL21(DE3) by pET-32a(+) vector. The results showed that the production of F-βD-3 protein was 127.23 μg/mL. After nickel column chromatography and enterokinase cleavage, the fusion protein production finally obtained was 18.17 μg/mL. Recombinant hβD-3 protein products were identified to possess inhibitory activity by bacteriostatic test on E. coli K₁₂D₃₁.