Experimental allergic encephalomyelitis in mice: encephalitogenicity of mouse central myelin basic proteins.

Abstract

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.

• Authors: H C Rauch, M Katar, I N Montgomery
• Journal: European journal of immunology (Eur J Immunol) Vol. 11 Issue 7 Pg. 545-9 (Jul 1981) ISSN: 0014-2980 [Print] Germany
• PMID: 6169533 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Amino Acids
• Myelin Basic Protein

Topics

• Amino Acids (analysis)
• Animals
• Central Nervous System (pathology)
• Chromatography, Ion Exchange
• Electrophoresis, Polyacrylamide Gel
• Encephalomyelitis, Autoimmune, Experimental (etiology, pathology)
• Guinea Pigs
• Mice
• Myelin Basic Protein (analysis, isolation & purification)