D D Wood, W J Vail, M A Moscarello
A non-penetrating reagent 4,4'-diisothiocyano-2,2'-ditritiostilbene disulfonic acid ([3H]DIDS) has been used to label isolated normal and diseased myelin. The basic protein and the hydrophobic protein, N-2, were isolated from each myelin. When normal myelin was labeled the specific activity of the basic protein was about 25% of that of the hydrophobic protein (N-2). The specific activities of these two proteins isolated from chronic multiple sclerosis myelin were similar to those of the normal myelin. In contrast, the specific acitivity of the basic protein isolated from acute multiple sclerosis myelin was about 400% higher than that of the basic protein isolated from either normal or chronic multiple sclerosis myelins...
August 15, 1975: Brain Research