Allergic encephalomyelitis. Isolation of an encephalitogenic peptide active in the monkey.
A 17-residue peptide (Peptide Y) was isolated from the COOH-terminal end of the basic protein of bovine myelin by peptic digestion. This peptide induced experimental allergic encephalomyelitis in the rhesus monkey. Treatment of Peptide Y with cyanogen bromide released three amino acids from the COOH-terminal end and resulted in a tetradecapeptide (Peptide M) which was also encephalitogenic in the rhesus monkey. The sequence of Peptide M is: Phe-Lys-LEU-Gly-Gly-Arg-Asp-Ser-Arg-Ser-Gly-Ser-Pro-Met. Thus a major disease-inducing site active in the rhesus monkey is contained within a 14-residue peptide localized near the COOH-terminal end of the protein. This peptide differs markedly in location and sequence from the 9-residue peptide shown to contain the encephalitogenic determinant for the guinea pig.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003488:Cyanogen Bromide; D004681:Encephalomyelitis, Autoimmune, Experimental / Q000139:chemically induced*; D008253:Macaca mulatta; D004676:Myelin Basic Protein / Q000302:isolation & purification*; D009186:Myelin Sheath; D010434:Pepsin A; D010455:Peptides / Q000378:metabolism*; D013329:Structure-Activity Relationship
D004676:Myelin Basic Protein; D010455:Peptides; D010434:Pepsin A; D003488:Cyanogen Bromide