Changes in Myelin Ultrastructure Produced by a Series of Physical and Chemical Agents
High-resolution electron microscopy of ultra-thin sections of fixed and plastic-embedded tissue shows that myelin consists essentially of an orderly aggregate of osmiophilic granules and osmiophobic globules. Frequently, granules and globules can be seen organized in hexagonal formations (diameter of about 90-120 A), which have an osmiophilic granule (diameter of about 30 A) in the center and six osmiophobic globules (diameter of about 40-45 A) around it. These formations are morphologically very similar to the “polyhedric-globular” (P-G) units (approx. 40-50 A high hexagonal prisms) which were described in the membrane of synaptic vesicles and mitochondria and in the plasma membranes of frog brain cortex as well as in the ribosomes of neurons of mammalian brain cortex. The P-G units were postulated to be an important, if not the exclusive, constituent of many biological membranes, which would be essentially a mosaic of such hexagonal prisms. Since ribosomes, which are believed to contain no lipid, also show the presence of P-G units in their structure, one wonders whether these units might possibly reflect mainly the presence of protein.