Recognition of liposome-bound antigens by antipeptide antibody
- 1 March 1993
- journal article
- research article
- Published by Springer Nature in Applied Biochemistry and Biotechnology
- Vol. 38 (3) , 179-188
- https://doi.org/10.1007/bf02916399
Abstract
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.Keywords
This publication has 7 references indexed in Scilit:
- Adsorption equilibrium in immunoaffnity chromatography with antibodies to synthetic peptidesBiotechnology & Bioengineering, 1990
- A simple method for measuring the complement activities of both classical and alternative pathways by using rabbit γ-globulin-coupled liposomesJournal of Fermentation and Bioengineering, 1989
- Immunogenicity of a free synthetic peptide: Carrier-conjugation enhances antibody affinity for the native proteinMolecular Immunology, 1987
- Covalent attachment of immunoglobulins to liposomes via glycosphingolipidsBiochimica et Biophysica Acta (BBA) - Biomembranes, 1981
- Monoclonal antibody covalently coupled to liposomes: Specific targeting to cellsJournal of Supramolecular Structure and Cellular Biochemistry, 1981
- A new enzymatic method for determination of serum choline-containing phospholipidsClinica Chimica Acta; International Journal of Clinical Chemistry, 1977
- The Serological Properties of Simple Substances. VII. A Quantitative Theory of the Inhibition by Haptens of the Precipitation of Heterogeneous Antisera with Antigens, and Comparison with Experimental Results for Polyhaptenic Simple Substances and for AzoproteinsJournal of the American Chemical Society, 1944