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Phylogenetically more conservative epitopes among monoclonal antibody-defined antigenic sites of human transferrin are involved in receptor binding
J. Bártek, V. Viklický, A. Stratil,
Language English Country England, Great Britain
Document type Journal Article
PubMed
2578807
Knihovny.cz E-resources
- MeSH
- Epitopes analysis MeSH
- Phylogeny * MeSH
- Carps MeSH
- Binding, Competitive MeSH
- Horses MeSH
- Rabbits MeSH
- Humans MeSH
- Antibodies, Monoclonal immunology MeSH
- Sheep MeSH
- Dogs MeSH
- Receptors, Cell Surface metabolism MeSH
- Receptors, Transferrin MeSH
- Cattle MeSH
- Transferrin immunology metabolism MeSH
- Cross Reactions MeSH
- Animals MeSH
- Check Tag
- Rabbits MeSH
- Humans MeSH
- Dogs MeSH
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
Of eight monoclonal antibodies raised against human transferrin, one (H.TF-14) cross reacted with pig and rabbit transferrins and one (H.TF-1) showed cross-reactivity with horse and dog transferrins. While rabbit and pig transferrins exhibited the same patterns of binding to MOLT-3 cell receptors as human and horse transferrins, binding of mouse and dog transferrins was weaker and bovine and carp transferrins gave entirely negative results. The results of these competitive binding experiments were confirmed by a biological test in which bovine transferrin had no effect on the growth of MOLT-3 cells when added to a serum-free medium. The observed correlation between cross-reactivity of anti-transferrin monoclonal antibodies and the binding abilities of transferrins to the MOLT-3 cell receptors may be associated with the conservatism of the part of the transferrin molecule recognized by the cell receptor.
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