title: [Extraction of membrane proteins in low ionic strengths].
abstract: Hemoglobin and the low molecular weight proteins 8 and 9 are extracted from ghosts during low ionic washing after the hypotonic hemolysis of erythrocytes. Furthermore, a loss of the proteins 4.5 and 7 was observed. The protein patterns of ghosts after isotonic hemolysis by freezing and thawing resemble the ghost protein patterns after hypotonic hemolysis and incomplete deprivation of Hb. Many if not all membrane proteins are eluted by repeated incubations of the ghosts in solutions of low ionic strength in the presence of EDTA. The spectrins, the proteins 5, 4.5, 7 and residual Hb are extracted preferentially. A selective extraction of the spectrins and the protein 5 is not detectable under these conditions. Often the spectrin bands are subdivided following low ionic incubation.
mesh_terms: D004492:Edetic Acid; D004910:Erythrocyte Membrane; D004912:Erythrocytes; D006461:Hemolysis; D006801:Humans; D008565:Membrane Proteins / Q000302:isolation & purification*; D008970:Molecular Weight; D013057:Spectrum Analysis
chemical_list: D008565:Membrane Proteins; D004492:Edetic Acid
vernacular_title: Extraktion von Membranproteinen bei niedrigen Ionenstärken.