亲和层析法提纯鸡马立克病毒gB基因重组产物

PURIFICATION OF RECOMBINANT GLUCOPROTEIN OF MAREK’S DIS-EASE VIRUS THROUGH AN AFFINITY COLUMN

应用针对鸡马立克病毒（ＭＤＶ）糖蛋白Ｂ（ｇＢ）抗原单克隆抗体ＩＡＮ８６制备亲和层析柱，从感染重组杆状病毒（ｇＢ－ＡｃＮＰＶ）的昆虫细胞中提纯鸡ＭＤＶｇＢ基因重组产物，获得较好效果。提纯的蛋白质在ＳＤＳ－ｐＡＧＥ中出现的５条条带中有４条在免疫印迹试验中出现，其分子量为１００，６０，４９，４０ｋｄ占蛋白总量的５４．７％。试验证明用单克隆抗体亲和层析法提纯ＭＤＶｇＢ基因重组产物是一个行之有效的方法。

The glucoprotein(gB)of Marey;disease virus(MDV)expressed in insect cell line Sf9 cells infected with recombi-nant baculovirus(gB-AcMNPV)was purified through an affinity column made of CNBr-Sepharose 4B linked with monocolonalantibody(MAb)IAN86 specific to MDV gB.The result of SDS-PAGE showed five main protein bands,of which molecularweight were separately 100,60,49,40,20kd.The fodhfour protein bands were sepecifically recognized by MAB IAN86 inwestern-blot,which occupied 54.7%of tatal protein.These results indicated that the purification procedure was effective. Usingthe purified products,we are going to investigate the biologlcal function of MDV gB.