Cross-reactivity of a monoclonal anti-[Met5]enkephalin antibody with cholecystokinin peptides.
The hypothesis of a conformational similarity between the unsulfated form of cholecystokinin C-terminal heptapeptide and [Met5]enkephalin was proposed by Schiller and colleagues. To test this possibility, we investigated the competition of cholecystokinin C-terminal peptides for the binding to a monoclonal anti-[Met5]enkephalin antibody. We observed that the antibody immunoprecipitated cholecystokinin peptides having at least the six C-terminal amino acids. Unlike the opiate receptors which had no affinity for the sulfated heptapeptide, the monoclonal antibody recognized the sulfated form of the C-terminal octapeptide of cholecystokinin.
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D002766:Cholecystokinin / Q000031:analogs & derivatives / Q000276:immunology*; D003429:Cross Reactions; D004744:Enkephalin, Methionine / Q000276:immunology*; D000939:Epitopes / Q000032:analysis*; D010446:Peptide Fragments / Q000276:immunology*; D013329:Structure-Activity Relationship
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D000939:Epitopes; D010446:Peptide Fragments; D004744:Enkephalin, Methionine; D002766:Cholecystokinin