Microheterogeneity of myelin basic proteins in the partially myelinated spinal roots of the Bar Harbor 129 ReJ muscular dystrophic mouse.
The protein composition of normal spinal roots and the partially myelinated spinal roots of Bar Harbor 129 ReJ dystrophic mice was analyzed by 2D-gel electrophoresis which resolved basic proteins. The normal roots contained proteins with mobilities identical to two of the three 18.5 kDa and two of the three 14 kDa myelin basic protein spots resolved in purified spinal cord myelin suggesting that normal root myelin may have some of the characteristics of CNS myelin. In contrast dystrophic roots contained spots with mobilities identical to only one of the spots resolved for each myelin basic protein. The possibility that the difference in microheterogeneity may be responsible for the decreased myelination is discussed.
Department of Genetics, Univesity of Edinburgh, U.K.
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John
D000818:Animals; D051379:Mice; D008970:Molecular Weight; D009137:Muscular Dystrophy, Animal / Q000378:metabolism*; D004676:Myelin Basic Protein / Q000032:analysis*; D009413:Nerve Fibers, Myelinated / Q000378:metabolism*; D013126:Spinal Nerve Roots / Q000378:metabolism*
D004676:Myelin Basic Protein