Synopsis
Electrophoretic analysis of multiple sclerosis plaques has disclosed the presence of a protein band with a mobility approximately the same as myelin proteolipid. The presence of this band was unexpected in view of the virtual absence of myelin from plaques. By application of histochemical staining procedures to electrophoretic ‘micro’ gels it has been shown that this plaque protein does not stain with Sudan Black (for lipid) and dimethylaminobenzaldehyde (for tryptophan) and cannot, therefore, be identified as normal proteolipid. The abnormal band is not associated with glial components or residual myelin within the plaque. We consider that this material might be a degradation product of myelin proteolipid formed during the demyelinating process.
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Csejtey, C., Hallpike, J.F., Adams, C.W.M. et al. Degraded proteolipid in multiple sclerosis plaques-histochemical electrophoretic observations. Histochem J 7, 599–604 (1975). https://doi.org/10.1007/BF01003797
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DOI: https://doi.org/10.1007/BF01003797