Hemoglobin-depleted human erythrocyte ghosts: characterization of morphology and transport functions.
A method of preparing hemoglobin-depleted resealed ghosts with an extremely low hemoglobin content is described. The membrane morphology, the crossed immunoelectrophoresis pattern of the membrane proteins, and the transport function of these ghosts have been examined. Electron microscopic examination of the ghosts on hydrophilic as well as hydrophobic grid surfaces revealed a faint filamentous network (spectrin) associated with the membrane. The ghosts were found to have permeabilities towards small polar molecules (water and mannitol) and ions (chloride, sodium, and potassium) which are quantitatively very close to those of intact red cells. It is concluded that white ghosts prepared by the present method are well suited for simultaneous studies of morphology, membrane biochemistry, and membrane transport functions.
D001693:Biological Transport, Active; D002458:Cell Fractionation / Q000379:methods; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000648:ultrastructure; D004912:Erythrocytes / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism; D006801:Humans; D007122:Immunoelectrophoresis; D008565:Membrane Proteins / Q000378:metabolism*; D008855:Microscopy, Electron, Scanning
D006454:Hemoglobins; D008565:Membrane Proteins