Monoclonal antibodies against hen's egg ovomucoid.
Two monoclonal antibodies (mAb 23E5 and 32A8) to hen's egg ovomucoid (OM), which causes hen's egg allergy and has trypsin inhibitory activity, were prepared and purified. Their affinity to the three separate domains of the ovomucoid, which are homologous in primary structure and are designated as DI, DII, and DIII, was studied by a competitive radioimmunoassay. MAb 23E5 bound to OM more efficiently than to DI, DII, or DIII-2 (with carbohydrate), but reacted with DIII-1 (free from carbohydrate) more efficiently than with OM. Except for the binding to OM, mAb 32A8 bound to DIII-2 most efficiently and to DIII-1 least efficiently, suggesting that this antibody recognized the carbohydrate moiety of DIII. MAb 32A8 inhibited the trypsin inhibitory activity of OM, whereas mAb 23E5 had no effect on it. These monoclonal antibodies should be useful for analyzing the antigenic determinants and trypsin inhibitory activity of ovomucoid.
Kaminogawa
S
S
Enomoto
A
A
Kurisaki
J
J
Yamauchi
K
K
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D000915:Antibody Affinity; D000918:Antibody Specificity; D002645:Chickens; D004527:Egg Proteins / Q000276:immunology*; D000939:Epitopes; D005260:Female; D010059:Ovomucin / Q000276:immunology*; D013329:Structure-Activity Relationship; D014361:Trypsin Inhibitors
D000911:Antibodies, Monoclonal; D004527:Egg Proteins; D000939:Epitopes; D014361:Trypsin Inhibitors; D010059:Ovomucin