Localization of Encephalitogenic Basic Protein in the Intraperiod Line of Lamellar Myelin

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IN the course of investigations on the immunogenic hypothesis of multiple sclerosis we have attempted the preparation of a “chemically pure myelin” and come to the conclusion that the giant molecular complex which composes the structure which the morphologist identifies as myelin has a certain integral molecular component which displays such a differentially high order of instability that this may be of great biological significance. A specific protein material is released rapidly post mortem from the intraperiod line of myelin and also from ultracentrifugally purified myelin in vitro, in conditions which make enzyme mediation improbable, and the myelin so obtained has a characteristic structure which we term “collapsed myelin”. Little else besides this protein seems to be released; and this protein has been shown to be a single entity identical with the “basic encephalitogenic protein” of central nervous tissue1–3.

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DICKINSON, J., JONES, K., APARICIO, S. et al. Localization of Encephalitogenic Basic Protein in the Intraperiod Line of Lamellar Myelin. Nature 227, 1133–1134 (1970) doi:10.1038/2271133a0

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