Characterisation of an epitope recognised by a monoclonal antibody against horse alcohol dehydrogenase using peptides synthesised on solid support.
Immunological analysis, using the Pepscan technique, of the tetradecapeptide, Pro344-Glu357 (PLITHVLPFEKINE), from horse liver alcohol dehydrogenase has identified a five amino acid sequence, HVLPF, which binds a monoclonal antibody. The epitope seems to be rather flexible with only two of the amino acids, Pro and Phe, having the characteristics of contact residues. However, the presence of the adjacent glutamic acid residue as part of the Pepscan peptide has a dramatic negative neighbourhood effect and inhibits binding. This highlights the potential risk of missing an epitope altogether when using the Pepscan procedure for epitope mapping.
Leone
N A
NA
International Institute of Genetics and Biophysics, CNR, Naples, Italy.
Whitehouse
D B
DB
Swallow
D M
DM
Wallace
G R
GR
Adinolfi
A
A
D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000276:immunology*; D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000918:Antibody Specificity; D000939:Epitopes / Q000276:immunology*; D006736:Horses; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000276:immunology
D000911:Antibodies, Monoclonal; D000939:Epitopes; D010455:Peptides; D000426:Alcohol Dehydrogenase