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[Epitope specificity of hemagglutinating monoclonal anti-A-antibodies].

Authors
  • Galanina, O E
  • Deriugina, E I
  • Lapenkov, M I
  • Nosyrev, A E
  • Korchagina, E Iu
  • Zamlianukhina, T V
  • Bovin, I V
Type
Published Article
Journal
Bioorganicheskaia khimiia
Publication Date
Mar 01, 1991
Volume
17
Issue
3
Pages
343–352
Identifiers
PMID: 1712202
Source
Medline
License
Unknown

Abstract

Fine epitope specificity of three anti-A monoclonal antibodies (MA) 1H410, 3F9, and 44F9 was studied by: 1) direct MA binding to synthetic oligosaccharides (OS) linked to polyacrylamide matrix, and 2) inhibition of MA binding to natural antigen by synthetic OS and their polyacrylamide conjugates. It has been established that the antigen binding site of MA 1H10 is specific for tetrasaccharide A (type 3), whereas MAs 3F9 and 44F9 recognize trisaccharide A, the contribution of alpha-L-fucosyl residue being insignificant in the case of 44F9 binding. The correlation of the MAs epitope specificity with their ability to agglutinate red blood cells of A1 and weak A subgroups is discussed.

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