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含ＥＢ病毒特异性ＤＮＡ酶全基因片段的大肠杆菌受变温诱导后，其上清液在十二烷基磺酸钠－聚丙烯酰胺凝胶电泳（ＳＤＳ－ＰＡＧＥ）时出现一条浓集带，分子质量大小约为５２ｋｕ，符合ＥＢ病毒ＤＮＡ酶全基因编码蛋白质大小。凝胶中蛋白质的定量扫描结果显示该蛋白质占宿主菌总蛋白质的２０％～２３％，实现了ＤＮＡ酶全基因在原核体系的高效表达。未见包涵体形成；迅速或缓慢升温所诱导目的蛋白质表达量基本相同。
Escherichia coli containing EBV-specific DNase gene fragment induced by temperature change, the supernatant of sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE) appeared a concentration zone, the molecular The quality of about 52ku, in line with Epstein-Barr virus DNA enzyme-encoded protein size. The quantitative analysis of the protein in the gel showed that the protein accounted for 20% ~ 23% of the total protein in the host bacteria, and the high expression of the whole DNase gene in the prokaryotic system was achieved. No inclusion body formed; rapid or slow warming induced by the same amount of protein expression.