Experimental allergic encephalomyelitis in mice: encephalitogenicity of mouse central myelin basic proteins.
Two co-extractable myelin basic proteins (MBP) were isolated and purified from mouse brain and designated: large (L), estimated to be composed of 160-164 amino acid residues, and small (S), estimated to contain 114-115 residues. The two proteins migrate separately in polyacrylamide gel electrophoresis (PAGE) in a pattern similar to rat MBP-S and MBP-L; mouse MBP-L resembles rat MBP-L, human, bovine and guinea pig MBP by PAGE and by amino acid analysis. This report demonstrates for the first time that mouse MPB-L alone, and not mouse MBP-S, is encephalitogenic for guinea pigs and mice.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002490:Central Nervous System / Q000473:pathology; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004681:Encephalomyelitis, Autoimmune, Experimental / Q000209:etiology* / Q000473:pathology; D006168:Guinea Pigs; D051379:Mice; D004676:Myelin Basic Protein / Q000032:analysis* / Q000302:isolation & purification
D000596:Amino Acids; D004676:Myelin Basic Protein