Chemical modifications of the protein of carcinoembryonic antigen: associated changes in immunological activity and conformation.
Chemical substitution of the exposed residues of tryptophan, tyrosine, histidine and arginine in carcinoembryonic antigen (CEA), using appropriately selective reagents, caused no significant change in the capacity of the antigen to bind to anti-CEA serum. However, treatments of CEA with 2-hydroxy-5-nitrobenzyl bromide and tetranitromethane, both in the presence of guanidine HCl, caused a large reduction in binding capacity. Measurement of the circular dichroism spectra of all of the products showed that retention of conformation of the molecular correlated well with retained antigenic activity, whereas the large losses in capacity to bind to anti-CEA sera were accompanied by a probably the result of gross conformational changes. The tyrosine residues of CEA may be classified into three categories: (i) 3 freely reacting residues, (ii) 7 or 8 moderately buried residues and (iii) 15 unreactive residues.
D000596:Amino Acids / Q000276:immunology; D001666:Binding Sites, Antibody; D002272:Carcinoembryonic Antigen; D055598:Chemical Phenomena; D002621:Chemistry; D002942:Circular Dichroism; D011487:Protein Conformation
D000596:Amino Acids; D002272:Carcinoembryonic Antigen