Characterization of epitopes on the cationic peanut peroxidase by four monoclonal antibodies.
The epitope sites on the cationic peanut peroxidase were characterized by four monoclonal antibodies raised against this isozyme. Evidence is presented showing that the epitope for monoclonal antibody 1B is located on the polypeptide. Sensitivity of the epitopes recognized by 1M and 2F to 0.1M HCl, boiling, 10 mM periodate and trifluoromethane sulfonic acid treatment indicate that they occur at regions where oligosaccharides are linked to the polypeptide backbone. The antigenic specificity of 2A is, in addition, dependent on the conformation of the epitope site which is destroyed after partial proteolysis of the peroxidase.
Hu
C F
CF
Department of Plant Sciences, University of Western Ontario, London, Canada.
van Huystee
R B
RB
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D010367:Arachis; D015153:Blotting, Western; D000939:Epitopes / Q000032:analysis*; D010447:Peptide Hydrolases; D010544:Peroxidases / Q000276:immunology*; D010944:Plants / Q000201:enzymology*
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D000939:Epitopes; D010544:Peroxidases; D010447:Peptide Hydrolases