Freeze-fracture properties of central myelin in the bullfrog.

The freeze-fractured membrane of the central myelin sheath has three classes of particulate components: (i) Particles inherent to the compact myelin lamellae. These are distributed at random and cleave predominantly with the P (protoplasmic) face. (ii) Particles which comprise the intramyelinic tight junctions. These are arranged in strands and are located at the inner and outer mesaxon, the paranodal loops, the cytoplasmic incisures, and occasionally within the compact regions of the myelin sheath. (iii) Particles localized exclusively at the portion of the paranodal loop membrane involved in the septate-like junction with the axolemma. These are regularly spaced and are organized in parallel rows. In the central myelin sheaths of bullfrogs fixed by perfusion with aldehydes and cryoprotected in 30% glycerol, the randomly distributed particles differ in size and shape from those of the axolemma. They possess a reasonably well defined bimodal distribution with respect to particle shape--most can be described either as globules or as ellipsoids. The globular particles range in diameter from 60 to 150 A. The ellipsoidal particles are 100-200 A long and 15-50 A wide. The total number of particles per square micron on the P face is approximately 1500. About half of these are of the globular type and half of the ellipsoidal type. In poorly fixed specimens, loss of interlamellar adhesion and loss of randomly distributed particles seem to coincide. Evidence is presented against the hypothesis that the tight junctions between compact myelin lamellae represent the radial component of the myelin. The possible relation between the types of particulate components seen in freeze-fracture and the classes of protein isolated from central myelin fractions is briefly discussed.