Richardson K, Parker C D
Infect Immun. 1985 Mar;47(3):674-9. doi: 10.1128/iai.47.3.674-679.1985.
Sodium dodecyl sulfate-urea polyacrylamide gel electrophoresis of outer membranes from a flagellated and an isogenic nonflagellated strain of Vibrio cholerae (classical, Inaba) suggested that two proteins were absent from the nonflagellated strain. Immunoblot examination of such preparations demonstrated that two proteins, present only in outer membrane from the flagellated strain, were associated with flagella. Analysis of purified flagellar cores from strains CA401 and N16961 (El Tor, Inaba) by electron microscopy, sodium dodecyl sulfate-urea polyacrylamide gel electrophoresis, and immunoblotting showed that these two proteins, with apparent molecular weights of 47,000 and 49,000, composed the flagellar core. Antiserum specific for flagellar core proteins did not agglutinate or inhibit the motility of intact V. cholerae. These latter findings suggested that, for intact cells, the flagellar core proteins are not accessible to antibody.
对霍乱弧菌(经典型,稻叶型)的一株有鞭毛菌株和一株同基因无鞭毛菌株的外膜进行十二烷基硫酸钠-尿素聚丙烯酰胺凝胶电泳分析,结果表明无鞭毛菌株中缺少两种蛋白质。对此类制剂进行的免疫印迹检测表明,仅存在于有鞭毛菌株外膜中的两种蛋白质与鞭毛相关。通过电子显微镜、十二烷基硫酸钠-尿素聚丙烯酰胺凝胶电泳和免疫印迹对CA401和N16961菌株(埃尔托生物型,稻叶型)的纯化鞭毛核心进行分析,结果显示这两种表观分子量分别为47000和49000的蛋白质构成了鞭毛核心。针对鞭毛核心蛋白的抗血清不会凝集或抑制完整霍乱弧菌的运动性。后一项发现表明,对于完整细胞而言,抗体无法接触到鞭毛核心蛋白。