粘液菌Distyotelium作为一种低等真核蛋白表达系统,能够高效表达外源蛋白。以Distyotelium和植物凝集素discoideum为标记构成的表达系统,所表达的融合蛋白可借助discoideum与半乳糖的特异结合性,通过琼脂糖凝胶Sephrose-4B进行过柱纯化。在外源蛋白和discoideum之间加上凝血酶切割位点,可利用凝血酶将过柱后的融合蛋白中的discoideum切去,而得到进一步纯化后的外源蛋白。 As a low-grade eukaryotic protein expression system, Distyotelium can express foreign proteins efficiently. Distyotelium and lectin discoideum as the marker expression system, the expression of the fusion protein can discoideum with galactose-specific binding by Sepharose-4B agarose gel column purification. Adding a thrombin cleavage site between the exogenous protein and discoideum, thrombin can be used to excise the discoideum in the post-columned fusion protein to obtain a further purified foreign protein.