Equilibrium and nonequilibrium competitive inhibitions of antipeptide antibody binding by parent myelin basic protein and 18 related peptide sequences

Equilibrium and nonequilibrium competitive inhibition analyses of a number of antisera to peptide S81 and S82 sequences were carried out through the use of inhibition radioimmunoassays with ¹²⁵I]S81, ¹²⁵I]S82, and ¹²⁵I]S79 and a panel containing 18 related peptides and five myelin basic protein preparations. Two principal determinants were identified, one of them sequential, the other nonsequential. The sequential determinant involved a peptide at or near the C-terminal end of S82 that could be blocked by an interchange of asparagine for glycine at the C terminus. The nonsequential determinant was dominant for a number of rabbit and rat antisera, both anti-S82 and anti-S81, and was shared not only by S81 and S82 but also by S8 and S80, i.e., the family of residues of bovine MBP sequence 69–83. Neither determinant was expressed in any of the myelin basic protein preparations, and the nonsequential determinant was not expressed in peptide sequences smaller than S8.