Dissociation of myelin from its 'enzyme markers' during ontogeny.
To avoid any loss of membranes, total particulate material prepared from the forebrain and spinal cord of rats of different ages was fractionated on linear sucrose gradients. Particle distribution, proteins and enzyme activities were measured. Beginning at early ages, optical density increases were observed around 0.60 M-sucrose, which corresponded to myelin deposition, and were expressed by the appearance of typical myelin proteins, which paralleled the peak activity of myelin-associated enzymes. During later development myelin proteins were found over a broad density range together with optical density shifts to higher (forebrain) and lower (spinal cord) values. In both regions myelin-associated enzymes shifted to heavier densities and were dissociated from the density region commonly considered to be compacted myelin.
D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000302:isolation & purification*; D000110:Acetylcholinesterase / Q000302:isolation & purification*; D000375:Aging; D000818:Animals; D002256:Carbonic Anhydrases / Q000302:isolation & purification*; D002490:Central Nervous System / Q000201:enzymology / Q000254:growth & development*; D002499:Centrifugation, Density Gradient; D004591:Electrophoresis, Polyacrylamide Gel; D009185:Myelin Proteins / Q000302:isolation & purification*; D010727:Phosphoric Diester Hydrolases / Q000302:isolation & purification*; D051381:Rats
D009185:Myelin Proteins; D000110:Acetylcholinesterase; D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases; D010727:Phosphoric Diester Hydrolases; D002256:Carbonic Anhydrases