Abstract
The history of basic protein in myelin from the central nervous system (CNS) is closely involved with the laboratory disease known as experimental allergic encephalomyelitis (EAE; Alvord, 1970). EAE was shown to be an autoimmune disease when Rabat et al. (1947) induced it in monkeys by injection of autologous brain tissue, together with appropriate adjuvants. Since then, many attempts have been made to isolate the active component of the CNS tissue responsible for disease induction. A number of fractions including phospholipids (Alvord, 1948), a complex cerebral lipid (Lumsden, 1949), an acetate-soluble material diffusible through cellophane (Hottle et al., 1949), a proteolipid fraction (Olitsky and Tal, 1952), a neurokeratin-like substance (Goldstein et al., 1953), a water-soluble collagen-like protein (Roboz et al., 1958), and a petroleum ether-soluble fraction (Lipton and Steigman, 1959) were all claimed to possess EAE-inducing (encephalitogenic) activity. However, a “salt”- or acid-extracted protein (Roboz and Henderson, 1959; Kies and Alvord, 1959) and a diffusible polypeptide fragment (Robertson et al., 1962) were later shown to be the most potent encephalitogens. The comparatively low activity of the other CNS tissue fractions was shown to be due to contamination with the acid-extracted protein and/or the polypeptide fraction (Kies et al., 1965; Kies, 1965; Lumsden et al., 1966).
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Dunkley, P.R., Carnegie, P.R. (1974). Isolation of Myelin Basic Proteins. In: Marks, N., Rodnight, R. (eds) Research Methods in Neurochemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7751-5_9
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