Development and characterization of monoclonal antibodies to chicken riboflavin carrier protein

Several monoclonal antibodies (MAbs) specific to chicken riboflavin carrier protein (cRCP) were developed and characterized. Of the several MAbs analy zed, four were directed against nonoverlapping epitopes as demonstrated by MAb inhibition assay. Many of these epitopes appeared to be in close proxim ity and only three were situated at distinct part of the molecule as reveal ed by sandwich assay. A combination of chemical modification, peptide cleav age by chemical and enzymatic methods, was used to analyze the possible ant igenic structure recognized by these MAbs. An assembled epitope spanning th e region 22-87 forms the antigenic site recognized by 4999.1; while MAb 555 5.3 interacted with the C-terminal peptide 203-219.