Recognition of liposome-bound antigens by antipeptide antibody.
In order to clarify the effects of the differences in physical states of antigens on recognition by antibodies in immunoassays, the binding characteristics of an antipeptide polyclonal antibody to the peptide and the corresponding protein were studied. The reactivity in the immunoliposome assay (ILA), as well as in the double-antibody sandwich ELISA, was identical to that in the solution. These results indicate that the conformation of liposome-bound antigen is changed little by coupling to liposomes and is almost the same as that of the native antigen in the liquid phase. It is desirable to assay by double-antibody sandwich ELISA or ILA to detect native proteins, and the latter is very easily performed.
Chemical Engineering Department, Faculty of Engineering, Kyoto University, Japan.
Y
Y
Sohma
R
R
Fujita
S
S
Katoh
E
E
Sada
D000818:Animals; D000906:Antibodies / Q000276:immunology*; D000937:Antigen-Antibody Reactions; D000941:Antigens / Q000276:immunology*; D004797:Enzyme-Linked Immunosorbent Assay; D007118:Immunoassay; D008081:Liposomes; D009211:Myoglobin / Q000276:immunology*; D010446:Peptide Fragments / Q000276:immunology*; D014907:Whales
D000906:Antibodies; D000941:Antigens; D008081:Liposomes; D009211:Myoglobin; D010446:Peptide Fragments