Literature DB >> 8373153

Recognition of liposome-bound antigens by antipeptide antibody.

Y Sohma1, R Fujita, S Katoh, E Sada.   

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.

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Year:  1993        PMID: 8373153     DOI: 10.1007/bf02916399

Source DB:  PubMed          Journal:  Appl Biochem Biotechnol        ISSN: 0273-2289            Impact factor:   2.926


  4 in total

1.  Adsorption equilibrium in immunoaffnity chromatography with antibodies to synthetic peptides.

Authors:  A Kondo; H Takamatsu; S Katoh; E Sada
Journal:  Biotechnol Bioeng       Date:  1990-01-20       Impact factor: 4.530

2.  Immunogenicity of a free synthetic peptide: carrier-conjugation enhances antibody affinity for the native protein.

Authors:  M Mariani; L Bracci; R Presentini; D Nucci; P Neri; G Antoni
Journal:  Mol Immunol       Date:  1987-03       Impact factor: 4.407

3.  Covalent attachment of immunoglobulins to liposomes via glycosphingolipids.

Authors:  T D Heath; B A Macher; D Papahadjopoulos
Journal:  Biochim Biophys Acta       Date:  1981-01-08

4.  Monoclonal antibody covalently coupled to liposomes: specific targeting to cells.

Authors:  J Barbet; P Machy; L D Leserman
Journal:  J Supramol Struct Cell Biochem       Date:  1981
  4 in total

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