Density and protein profiles of myelin from two regions of young and adult rat CNS.

Myelin, isolated from forebrain and spinal cord of young and adult rats, was distributed by zonal centrifugation on linear (0.32--1.00 M) sucrose gradients in a bell-shaped mode. The peak position of forebrain myelin shifted from the density of 0.58 M sucrose in young animals to that of 0.67 M sucrose in adult rats, while in spinal cord no such pronounced shift was noticed (approximately 0.58 M sucrose). Morphologically, the preparations appeared very similar across the density ranges. Specific activities of acetylcholinesterase were substantially below the total homogenates, while those of 2', 3'-cyclic nucleotide 3'-phosphohydrolase were higher in all fractions, except in the light myelin subfractions from adult spinal cord. Basic proteins decreased from the light to the heavier fractions; higher molecular weight proteins increased, together with proteolipid protein, which in spinal cord reached a plateau and in forebrain decreased towards the heavy side. The ratio of the small basic protein/large basic protein showed higher values in the light myelin subfractions in the regions and ages examined, pointing to a higher degree of maturation.