{'fraction_non_alphanumeric': 0.032134659525631215, 'fraction_numerical': 0.006885998469778117, 'mean_word_length': 5.055555555555555, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Studies on the species-variability of experimental allergic encephalomyelitis in guinea pigs and rats.


 The present investigation was carried out to compare myelin basic protein (BP) isolated from guinea pig and rat central nervous system with respect to physicochemical properties and ability to induce experimental allergic encephalomyelitis (EAE) in Hartley guinea pigs and Lewis rats. The single BP tryptophan residue was modified with 2-hydroxy-5-nitrobenzyl bromide (benzyl-BP). Polyacrylamide gel electrophoresis at acid pH or in sodium dodecyl sulfate (SDS) revealed that mobility and molecular size, respectively, were not changed by modifying the tryptophan residue. Guinea pig and rat BP, and each respective benzyl-BP, were highly encephalitogenic in rats, as was the purified small rat basic protein (rat-S). However, the peptide derived from the N-terminal end of the BP molecule by cyanogen bromide cleavage (CB-1) was completely inactive in rats. Guinea pig and rat BP were also highly encephalitogenic in guinea pigs, but the benzyl-BP preparations were relatively inactive. Rat-S and CB-1 were only mildly encephalitogenic. It appears that the determinant which induces EAE in rats is located between BP residues 21 and 115. The guinea pig recognizes at least two disease-inducing sites.