Alexander A G, Lowes H R, Kenny G E
Department of Biology, Pacific Lutheran University, Tacoma, Washington 98447-0003.
Infect Immun. 1991 Jun;59(6):2147-51. doi: 10.1128/iai.59.6.2147-2151.1991.
Immunoblotted protein samples from several strains of Mycoplasma hominis and from one strain of Mycoplasma arginini each contain a polypeptide of a molecular mass of 95,000 to 105,000 Da which binds immunoglobulin nonimmunologically. Immunoblots from these organisms were probed with alkaline phosphatase-conjugated goat anti-rabbit immunoglobulin, conjugated goat immunoglobulin G (IgG) Fab fragments, and conjugated goat IgG Fc fragments. The polypeptide bound the goat anti-rabbit molecules and the Fab fragments but not the Fc fragments. These reactions could be blocked with nonimmune unconjugated goat IgG and unconjugated human IgM. Controls probed with alkaline phosphatase alone did not stain. Binding of the conjugated preparations to whole mycoplasmal cells was dependent on concentrations of both conjugate and cells for the goat anti-rabbit preparation and for Fab. The mycoplasmal polypeptide may be a light-chain-specific reactant.
来自几株人型支原体以及一株精氨酸支原体的免疫印迹蛋白样品均含有一种分子量为95,000至105,000道尔顿的多肽,该多肽能非免疫性地结合免疫球蛋白。用碱性磷酸酶偶联的山羊抗兔免疫球蛋白、偶联的山羊免疫球蛋白G(IgG)Fab片段以及偶联的山羊IgG Fc片段对这些支原体的免疫印迹进行检测。该多肽能结合山羊抗兔分子和Fab片段,但不能结合Fc片段。这些反应可被非免疫未偶联的山羊IgG和未偶联的人IgM阻断。仅用碱性磷酸酶检测的对照未显色。对于山羊抗兔制剂和Fab,偶联制剂与完整支原体细胞的结合取决于偶联物和细胞的浓度。支原体多肽可能是一种轻链特异性反应物。