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使用ＫＣＮＳ解离、硫酸铵沉淀、电泳制备分离并纯化了鼠疫菌ｐＨ６抗原。ＳＤＳ－ＰＡＧＥ图型显示，提取物为单一蛋白，参照标准，推算其分子最约１５ｋＤ。多数情况下，在其上方尚有一条含最较低、表征分子量约１６ｋＤ的蛋白带，用Ｆ１单克隆抗体及１５ｋＤ蛋白制备的抗血清分别进行测定，该蛋白仅能与１５ｋＤ蛋白的抗血清产生高滴度反应，从而排除了其为Ｆ１抗原的可能性。依据上述实验结果并结合ＬｉｎｄｌｅｒＬＫ等的资料分析，该蛋白与提纯抗原属同一物质，表征分子量间的差异，很可能是分子量较大的一种（约１６ｋＤ）带有一段１ＫＤ的信号序列所致。用精制的ｐＨ６抗原免疫小鼠４只，所有小鼠于初次免疫后的第３０天放血测定，均与提纯抗原出现了高滴度的阳性反应，说明尽管提纯蛋白的方法不够温和，有可能使蛋白发生变性，但其免疫原性基本不受影响，做一般使用时可不做复性处理。
The Yersinia pestis pH6 antigen was isolated and purified using KCNS dissociation, ammonium sulfate precipitation and electrophoresis. SDS-PAGE patterns show that the extract is a single protein, reference standard, calculate the molecular maximum of about 15kD. In most cases, there is a band containing the lowest protein band of about 16 kD, measured with an F1 monoclonal antibody and a 15 kD protein antiserum, which is only capable of producing antiserum with a 15 kD protein High titer reaction, thus ruled out the possibility of its F1 antigen. Based on the above experimental results and analysis of data from LindlerLK, the protein is identical to the purified antigen and characterizes the difference between the molecular weights, probably due to a larger molecular weight (about 16 kD) with a 1KD signal sequence. Four mice were immunized with the purified pH6 antigen. All mice were bled at day 30 after the first immunization and both showed high titers of positive reaction with the purified antigen, indicating that although the protein purification method is not mild enough, it is possible to Protein denaturation, but its basic immunogenicity is not affected, so do not do the normal use of rendezvous.