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Thermally Induced Epitope Regions of Ovalbumin Identified with Monoclonal Antibodies
Author(s) -
IKURA K.OJI,
HIGASHIGUCHI F.UMIHARU,
KITABATAKE N.AOFUMI,
DOI E.TSUSHIRO,
NARITA H.IROSHI,
SASAKI R.YUZO
Publication year - 1992
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1992.tb08059.x
Subject(s) - ovalbumin , epitope , monoclonal antibody , denaturation (fissile materials) , chemistry , antibody , biochemistry , microbiology and biotechnology , biology , antigen , immunology , nuclear chemistry
To identify the structural regions of the ovalbumin molecule that change during heat denaturation, we used monoclonal antibodies that reacted specifically with the soluble heat‐denatured ovalbumin as probes. Five monoclonal antibodies recognizing different epitopes of the denatured ovalbumin were produced. Through the isolation and sequence analysis of the peptides derived from ovalbumin that reacted with the monoclonal antibodies, five parts of the ovalbumin molecule were identified as the regions that change structurally and provide new epitopes during heat denaturation. These findings could be useful information in understanding the structural properties of heat‐denatured ovalbumin.