Allergic encephalomyelitis: evidence for lack of significant encephalitogenic activity of purified peptide L in the monkey

Abstract

peptide L was further cleaved by cyanogen bromide, two peptides, peptide J (residues 1-20) and peptide D (residues 21-115), were obtained. Peptide J was inactive in inducing EAE, while peptide D was as weakly active as peptide L. Conformational studies and identical rate of tryptic hydrolysis Experimental allergic encephalomyelitis is an autoimmune disease induced by the basic protein of CNS* 1 myelin (Laatsch et al., 1962;Einstein et al., 1962; which comprises 30% of the total myelin protein. The protein is believed to have a highly ordered and folded structure and is best described as a prolate ellipsoid with an axial ratio 10:1 (Epand et al., 1974). The ease with which the basic protein can be isolated from myelin suggests that its location in the membrane is that of a so-called peripheral protein. The determination of the amino acid sequence of this protein has facilitated the definition of different encephalitogenic sites in this protein which are: a nonapeptide (residues 113-121

In healthy primates, circulating autoreactive T cells mediate autoimmune disease.

“…Mapping data in C. jacchus are in agreement with a previous report suggesting that the carboxy terminus of MBP contains antigenic determinants in primates (26) but also indicates that the natural encephalitogenic repertoire in C. jacchus is broad. In most inbred rodents examined, only exceedingly restricted populations of T cells mediate acute EAE.…”

Immunological Aspects of Demyelinating Diseases

“…and 84-102 (125) which were recognized in the context of one of the polymorphic beta chains of HLA DRwI5, HLA-DR2b (134), and HLA-DQBl (125) probably all contain similar core sequences. AA 153-165 in the rhesus monkey (137) and AA 1�9Ac in PL/J and BlO.PL mice (30, 59-6 1). AA 153-165 in the rhesus monkey (137) and AA 1�9Ac in PL/J and BlO.PL mice (30, 59-6 1).…”

DNA-containing membrane vesicles of Pseudomonas aeruginosa PAO1 and their genetic transformation potential

“…KDO (3-deoxy-D-manno-octulosonic acid) was determined by the thiobarbituric acid method (Karkhanis et al, 1978) with purified KDO (Sigma) as a standard.…”