Intramembrane particle aggregation in erythrocyte ghosts. I. The effects of protein removal.
We have used freeze-etching and SDS-polyacrylamide gel electrophoresis to study the conditions under which the intramembrane particles of the human erythrocyte ghost may be aggregated. The fibrous membrane protein, spectrin, can be almost entirely removed from erythrocyte ghosts with little or no change in the distribution of the particles. However, after spectrin depletion, particle aggregation in the plane of the membrane may be induced by conditions which cause little aggregation in freshly prepared ghosts. This suggests that the spectrin molecules form a molecular meshwork which limits the translational mobility of the erythrocyte membrane particles.
D001798:Blood Proteins; D002462:Cell Membrane / Q000032:analysis / Q000648:ultrastructure; D004589:Electrophoresis, Disc; D004912:Erythrocytes; D005613:Freeze Etching; D005976:Glutaral; D006801:Humans; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008954:Models, Biological; D009439:Neuraminidase; D009994:Osmolar Concentration; D011506:Proteins / Q000378:metabolism; D012965:Sodium Chloride; D013696:Temperature; D014357:Trypsin
D001798:Blood Proteins; D046911:Macromolecular Substances; D011506:Proteins; D012965:Sodium Chloride; D009439:Neuraminidase; D014357:Trypsin; D005976:Glutaral