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将人血红蛋白α、β珠蛋白基因分别克隆进 pET 2 1b原核表达载体中 ,宿主菌经IPTG化学诱导 ,在1.6× 10 5处有特异的蛋白带表达。表达产物以可溶形式存在 ,α珠蛋白的表达量达总菌体蛋白的 5 % ,β珠蛋白的表达量达 15 % ,并经Western Blotting杂交证实。
The human hemoglobin α and β globin genes were cloned into pET 2 1b prokaryotic expression vector respectively. The host bacteria were induced by IPTG and expressed at 1.6 × 10 5. The expression product was in soluble form. The expression of alpha-globin was 5% of the total bacterial protein and the expression of beta-globin reached 15%, which was confirmed by Western Blotting.