Abstract
Abstract Human red blood cell ghosts are severely disrupted by the removal of inorganic cations, and in the presence of 5 x 10-3 m EDTA or 0.1 m (CH3)4NBr the membrane proteins are almost totally soluble in aqueous media without the use of detergents or organic solvents. These soluble proteins have been partially fractionated by column chromatography as a preliminary step to studying their physical and functional properties. Optical rotatory dispersion spectra indicate no major conformational change upon removal of the proteins from the insoluble lipid in the solvent systems studied. Preliminary investigation of porcine cerebral myelin and bovine heart inner mitochondria suggest that the interaction between lipid and protein differs in these two systems from that in the human erythrocyte membrane.
Highlights
Human red blood cell ghosts are severely disrupted by the removal of inorganic cations, and in the presence of 5 x 10V3 M EDTA or 0.1 M (CHp)dNBr the membrane proteins are almost totally soluble in aqueous media without the use of detergents or organic solvents
Solubility of Proteins in Aqueous JJedia-Fresh human red blood cell ghosts were suspended in varying concentrations of EDTA, 5 x low4 M azide, pH 7.5, as described under “Experimental Procedure.”
It is significant that the maximum amount of protein is solubilized in 5 x lop3 M EDTA and that increasing the concentration of this chelating agent reduced the yield of soluble protein
Summary
Human red blood cell ghosts are severely disrupted by the removal of inorganic cations, and in the presence of 5 x 10V3 M EDTA or 0.1 M (CHp)dNBr the membrane proteins are almost totally soluble in aqueous media without the use of detergents or organic solvents These soluble proteins have been partially fractionated by column chromatography as a preliminary step to studying their physical and functional properties. Since one would like to find some generality in the organization of and forces in biological membranes, we include some preliminary comparative studies on porcine cerebral myelin and bovine heart inner mitochondrial membrane These investigations suggest differences in the protein-lipid interaction in the three membrane systems
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