Membrane particles on fracture faces of frozen myelin.
AUTOR(ES)
da Silva, P P
RESUMO
Freeze-fracture electron microscopy reveals constant and widespread presence of membrane particles on the fracture faces of frozen myelin. In unfixed myelin frozen shortly after dissection the distribution of the particles is uniform. In glutaraldehyde-fixed and/or glycerol-impregnated myelin the particles frequently occupy a network interspersed with circumscribed particle-free areas of variable dimension. In these membranes the network of particles is propagated radially across many lamellae. Particle-rich areas are closely apposed and contrast with frequent delamination of adjacent particle-free regions. We propose that, as in other plasma membranes, the particles of myelin represent protein-containing structures intercalated across the hydrophobic matrix of a membrane with bilayer organization. Our results indicate that these structures contain sites which mutually interact at the surface of apposed membranes and may be important in maintaining the organizational integrity of myelin.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=433135Documentos Relacionados
- Fracture faces of frozen membranes.
- Linear arrays of intramembranous particles in pulmonary tubular myelin.
- Fracture-label:O cytochemistry of freeze-fracture faces in the erythrocyte membrane.
- The structure of bovine brain myelin proteolipid and its organization in myelin.
- Structure and molecular arrangement of proteolipid protein of central nervous system myelin.
