Sugii S, Tajima T
Department of Veterinary Science, College of Agriculture, Osaka Prefecture University, Japan.
J Vet Med Sci. 1998 Nov;60(11):1255-7. doi: 10.1292/jvms.60.1255.
The reactivity of native bovine conglutinin (Kg) with antibody against recombinant Kg (rKg), with deletion of the N-terminal and collagen-like regions of the native Kg molecule, was studied by sandwich enzyme-linked immunosorbent assay. With anti-recombinant Kg antibody as the coating antibody, rKg reacted with biotinylated homologous anti-rKg and heterologous anti-Kg antibodies as probing antibodies, while native Kg did not. With anti-native Kg antibody as coating antibody, native Kg reacted with biotinylated homologous antibody as probing antibody, while recombinant Kg reacted weakly with both biotinylated homologous and heterologous antibodies. Consequently the N-terminal and collagen-like regions of native Kg molecule are essential to express the complete immunogenicity and/or antigenicity of the native Kg molecule.
通过夹心酶联免疫吸附测定法,研究了天然牛凝集素(Kg)与针对重组Kg(rKg)的抗体之间的反应性,该重组Kg缺失了天然Kg分子的N端和胶原样区域。以抗重组Kg抗体作为包被抗体时,rKg与生物素化的同源抗rKg和异源抗Kg抗体作为检测抗体发生反应,而天然Kg则不反应。以抗天然Kg抗体作为包被抗体时,天然Kg与生物素化的同源抗体作为检测抗体发生反应,而重组Kg与生物素化的同源和异源抗体反应均较弱。因此,天然Kg分子的N端和胶原样区域对于表达天然Kg分子的完整免疫原性和/或抗原性至关重要。