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采用酸解法、单抗亲和层析提纯了鼠伤寒沙门氏菌（Ｓ．ｔｙｐｈｉｍｕｒｉｕｍ）鞭毛蛋白Ｈｉ。经电镜和ＳＤＳＰＡＧＥ鉴定，发现４２ｋＤ的蛋白带，即鞭毛蛋白（Ｆｌａｇｅｌｌｉｎ）。它能够刺激小鼠产生特异性抗体，酶联免疫吸附试验（ＥＬＩＳＡ）、凝集试验（ＤＡ）测定其Ｈｉ抗体效价分别为１：１０４、１：１０３。用其他非Ｈｉ抗原的沙门氏菌包板，ＥＬＩＳＡ效价可达１：１００～１：１０００，ＤＡ阴性。这表明沙门氏菌鞭毛蛋白上存在着属特异共同抗原表位，且免疫原性较好，该类表位免疫性比分型Ｈ抗原弱，提示沙门氏菌分型Ｈ抗原表位是鞭毛蛋白分子上的优势表位。用沙门氏菌鞭毛蛋白属特异共同抗原表位单抗ｄｅ７研究被动保护作用，结果显示该表位被动保护作用很小。本研究为沙门氏菌鞭毛蛋白抗原多样性及特性研究提供了新的认识，并为临床上诊断沙门氏菌感染提供了新的检测对象。
The S. typhimurium flagellin Hi was purified by acid hydrolysis and monoclonal antibody affinity chromatography. Electron microscopy and SDSPAGE identification, found 42kD protein band, flagellin (Flagellin). It can stimulate mice to produce specific antibodies. The antibody titer of Hi antibody was 1: 104,1: 103 by enzyme-linked immunosorbent assay (ELISA) and agglutination test (DA) respectively. With other non-Hi antigen Salmonella package plate, ELISA titer up to 1: 100 ~ 1: 1000, DA negative. This indicates that Salmonella flagellin belongs to a specific common antigen epitope and has good immunogenicity. The immunogenicity of the epitopes is weaker than that of the type H antigen, which indicates that the Salmonella typing H antigen epitope is a superiority list on the flagellin molecule Bit. Salmonella flagellin is a specific common epitope monoclonal antibody de7 study of passive protection, the results showed that the epitope passive protection is small. This study provided a new understanding of the diversity and characterization of Salmonella flagellin antigen and provided a new test object for clinical diagnosis of Salmonella infection.