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- W2013144034 abstract "CNS myelin was prepared by six different gradient systems. The purity of the preparations was evaluated by electron microscopy and chemical markers. Electron-microscopic analysis of crude myelin preparations revealed contamination by axonal contents, mitochondria and lysosomes, while final preparations were characterized by small myelin fragments with little or no contamination. Chemical analysis revealed an approximately 500–1000-fold decrease in soluble, mitochondrial and lysosomal markers. The final preparations revealed a typical myelin structure and an absence of significant contamination by DNA. 7–14% of the neutral proteinase activity of the crude brain homogenate was found in purified myelin. This may favour the possibility that a part of the neutral proteinase is intimately linked to the myelin. The possible function of neutral proteinase in the formation of myelin buds during demyelination is discussed." @default.
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- W2013144034 modified "2023-10-16" @default.
- W2013144034 title "Further studies on neutral proteinase activity of CNS myelin" @default.
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- W2013144034 doi "https://doi.org/10.1016/0006-8993(70)90435-x" @default.
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