Publications by authors named "A K Yazova"
Article Synopsis
- Alpha-fetoprotein (AFP) is a protein found in mammalian blood during embryonic development, consisting of a single glycosylated chain with multiple epitope clusters.
- Researchers developed three methods for separating variants of AFP based on different epitope expressions using technologies like immunoaffinity electrochromatography and electrophoresis/immunoblotting.
- The techniques allowed for the identification of hidden (cryptic) epitopes in AFP, which has important implications that are explored in the study's findings.
Expression of two conformationally dependent epitopes (cdes) designated as cdeD and cde106 of human alpha-fetoprotein (hAFP) was studied in hAFP of fetal and tumor origin. This was done by immunoaffinity electrochromatography on nitrocellulose membrane and by ELISA. Using anti-cdeD and anti-cde106 monoclonal antibodies (MoAbs), the relationship between the cde-positive and cde-negative hAFP fractions was evaluated in 75 samples with the above techniques.
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- The study investigated the epitope structure of human alpha-fetoprotein (AFP) using over 50 monoclonal antibodies from international workshops.
- Researchers analyzed the AFP-antibody interactions through competitive immunoaffinity electrochromatography on nitrocellulose membranes, identifying five types of interactions including complete and partial neutralization.
- The findings led to the creation of an epitope map for AFP, highlighting 23 distinct epitopes and discussing the implications of these interactions on the AFP molecule's structure.
The immunological heterogeneity of human alpha-fetoprotein (AFP) was demonstrated using immunoaffinity electrochromatography on monoclonal antibodies (MoAbs) to 3 non-cross-reacting epitopes of this protein. At least 4 subfractions expressing different epitopes were found in the native AFP. These subfractions demonstrated molecular weights similar to the major component of the original AFP.
View Article and Find Full Text PDFThirty monoclonal antibodies (MoAbs) to human alpha-fetoprotein (AFP) were compared with one another by two methods: Immunoaffinity electrochromatography or additive ELISA. The first method permitted to analyse the epitopes of native AFP in solution [Abelev et al., Immunol Lett 1994;40:133-138] while the other approach also detects the epitopes of conformationally modified (partly denatured) AFP fixed on the plastic [Yazova et al.
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