Abstract
Brain stem slices from actively myelinating rats were incubated 30 min with [ 3H]leucine, then the labeling of proteins was halted by a chase with cold amino acid and slices incubated for an additional 30 min. Proteins from 10 particulate fractions of the tissue dispersion were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and bands corresponding to five major myelin proteins were analyzed. All proteins appeared in myelin after an initial time lag and the labeling continued after the chase, although distinct differences between integral and peripheral myelin proteins regarding the kinetics of entry were observed. Labeling of proteins in a subcellular fraction in the chase experiment was used to determine the localization of the fraction along the intracellular route of myelin protein flow. The data support the contention of precursor-product relationships between myelin subfractions and myelin-like membranes. The involvement of other particulate fractions in processing myelin proteins is considered.
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