Distribution of transmembrane polypeptides in freeze fracture.
Human erythrocytes have been freeze-fractured, and the polypeptides associated with the separate halves of the membrane bilayer have been analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The transmembrane proteins were differentially separated by the fracture process. Although sialoglycoproteins associated with the outer half of the membrane, the anion transport protein (band 3) mainly remained with the inner half of the membrane. Well-defined fragments of the sialoglycoproteins were produced by the freeze-fracture procedure, indicating that selected covalent bonds of these transmembrane proteins were broken.
D004910:Erythrocyte Membrane / Q000648:ultrastructure*; D004912:Erythrocytes / Q000648:ultrastructure*; D005614:Freeze Fracturing / Q000379:methods; D006023:Glycoproteins / Q000097:blood; D006801:Humans; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000097:blood; D008970:Molecular Weight; D011107:Polylysine; D011485:Protein Binding; D011487:Protein Conformation
D006023:Glycoproteins; D046911:Macromolecular Substances; D008565:Membrane Proteins; D011107:Polylysine