Blackall P J, Rogers D G, Yamamoto R
Department of Primary Industries, Animal Research Institute, Yeerongpilly, Australia.
Avian Dis. 1990 Oct-Dec;34(4):871-7.
The outer-membrane protein (OMP) profiles of four isolates of Haemophilus paragallinarum (0083, 0222, Modesto, and HP31) were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. OMPs were isolated by sonic disruption followed by differential centrifugation and selective solubilization in Triton X-100. Although the isolates had similar profiles overall, two distinct OMP profile types, based on the variable molecular weight of a protein termed OMP C (39,000 or 38,000), were found. In addition, OMP C was found to be a heat-modifiable protein--being either absent or present in only minor amounts if the preparations were not heated at 100 C. Major and minor OMPs, some common to all four isolates, were recognized in immunoblots by an immune serum to isolate HP31.
通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳对副鸡嗜血杆菌的4个分离株（0083、0222、莫德斯托和HP31）的外膜蛋白（OMP）图谱进行了检测。通过超声破碎，然后差速离心，并在Triton X-100中选择性溶解来分离OMP。尽管这些分离株总体上具有相似的图谱，但基于一种称为OMP C（39,000或38,000）的蛋白质分子量的变化，发现了两种不同的OMP图谱类型。此外，发现OMP C是一种热可修饰蛋白——如果制剂不加热到100℃，则不存在或仅少量存在。在免疫印迹中，用针对分离株HP31的免疫血清识别出了主要和次要的OMP，其中一些是所有4个分离株共有的。
