Rhodopsin's amino terminus is a principal antigenic site.

Antisera and monoclonal antibodies to rhodopsin were examined for their binding specificity to rhodopsin by using peptides from the rhodopsin sequence as competitors for antibody binding to rhodopsin in an enzyme-linked immunoassay. Monoclonal antibodies tested were raised in mice against bovine and rat rhodopsin. Antisera tested were raised in sheep against bovine rhodopsin and in rabbits against human rhodopsin. Peptides were synthesized from the bovine rhodopsin sequences 2-32, 1-12, 13-23, 24-34, 5-11, 231-252 and 331-348 for use as competitors in the immunoassay. A mixture of soluble CNBr peptides, and the purified CNBr peptide representing the sequence 2-39 were also employed. The monoclonal antibodies were all anti-amino-terminal in their binding specificity, although each recognized slightly different regions of the amino terminus. Each of the three antisera was predominantly directed against rhodopsin's amino terminus. We conclude that the amino-terminal 30 or more amino acids, and particularly the amino-terminal 15 amino acids, represent a principal antigenic region of the rhodopsin molecule.