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The basic protein of bovine central nervous system myelin contains a single polypeptide chain of 170 amino acids. Multiple components of basic protein have been observed on disc gel electrophoresis and ion exchange chromatography at alkaline pH, but the basis of the microheterogeneity has not been established. In the present study myelin basic protein from(More)
Peptide C1 (residues 68-88) from GP and rat BP differ by a single amino acid interchange at residue 79. This residue is serine in GP C1 and threonine in rat C1. GP C1 was encephalitogenic in Le rats at doses as low as 15 ng. Rat C1 was encephalitogenic at doses of 1,500 ng or greater. LNC from rats challenged with 25 X 10(-4) micronmol of GP C1 and 250 X(More)
A series of peptides, produced from peptide 68-88 by selective enzyme cleavage, were used to define the amino acid sequences required for the induction of experimental allergic encephalomyelitis (EAE), an in vitro lymphocyte proliferative response (LPR), and serum antibody by peptide 68-88 in the Lewis rat. Here we present data that indicate that the T cell(More)
Lewis rats were used to determine the encephalitogenic activity of myelin basic protein of different species and of 45-residue fragments of basic protein. Basic protein from guinea pigs was more active than that from rats, and the fragments from the two species showed the same order of activity. Bovine basic protein was the least active of the intact(More)