Hansen E J, Frisch C F, Johnston K H
Infect Immun. 1981 Sep;33(3):950-3. doi: 10.1128/iai.33.3.950-953.1981.
A radioimmunoprecipitation method has been devised which permits the direct identification of those proteins which are both exposed on the cell surface of Haemophilus influenzae type b and accessible to antibody. Both extrinsically and intrinsically radiolabeled cells of this organism were employed as the sources of antigen in radioimmunoprecipitation experiments which involved incubation of intact bacterial cells with antisera. Several different proteins, ranging in apparent molecular weight from 33,000 to 160,000, were shown to be accessible to antibody on the cell surface of this pathogen.
已经设计出一种放射免疫沉淀方法,该方法可以直接鉴定那些既暴露于b型流感嗜血杆菌细胞表面又能与抗体结合的蛋白质。在放射免疫沉淀实验中,将这种生物体的外在和内在放射性标记细胞都用作抗原来源,实验包括完整细菌细胞与抗血清的孵育。结果显示,几种不同的蛋白质,其表观分子量在33,000至160,000之间,可在这种病原体的细胞表面与抗体结合。