Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Proceedings, annual meeting, Electron Microscopy Society of America
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
