Chart H, Griffiths E
J Gen Microbiol. 1985 Jun;131(6):1503-9. doi: 10.1099/00221287-131-6-1503.
The ferric enterobactin receptor protein (81 kDal) of Escherichia coli O111 was purified by preparative sodium dodecyl sulphate-polyacrylamide gel electrophoresis and used to raise polyclonal antiserum in rabbits. This antiserum was used in conjunction with the immunoblot technique to examine the degree of antigenic homology of the ferric enterobactin receptor protein among 17 pathogenic and laboratory strains of E. coli. Both the molecular weight and the antigenic properties of the enterobactin receptor were highly conserved. However, the laboratory strain C and a pathogenic enteroinvasive strain, E. coli O164, were unusual in not producing the 81 kDal protein. The antiserum also recognized an 81 kDal protein from iron-restricted Salmonella typhimurium and an 83 kDal protein from iron-restricted Klebsiella pneumoniae.
通过制备性十二烷基硫酸钠-聚丙烯酰胺凝胶电泳纯化了大肠杆菌O111的铁肠杆菌素受体蛋白（81 kDa），并用于在兔中制备多克隆抗血清。该抗血清与免疫印迹技术结合使用，以检测17株致病性和实验室菌株的大肠杆菌中铁肠杆菌素受体蛋白的抗原同源程度。肠杆菌素受体的分子量和抗原特性都高度保守。然而，实验室菌株C和致病性侵袭性菌株大肠杆菌O164不同寻常，它们不产生81 kDa蛋白。该抗血清还识别来自铁限制型鼠伤寒沙门氏菌的81 kDa蛋白和来自铁限制型肺炎克雷伯菌的83 kDa蛋白。
