The permeability of bilayer lipid membranes on the incorporation of erythrocyte membrane extracts and the identification of the monosaccharide transport proteins.
1. Extracts of the human erythrocyte membrane have been prepared by five different procedures involving Triton X-100 solubilization and gel chromatography. 2. The extracts have been analysed by gel electrophoresis and incorporated asymmetrically into phosphatidylcholine-cholesterol-n-decane planar bilayers. 3. Removal of excess Triton X-100 from membrane extracts or prolonged storage facilities the proteolysis of membrane extracts with the partial or complete breakdown of band 3 polypeptides (notation of Fairbanks, G., Steck, T.L. and Wallach, D.F.H. (1971) Biochemistry 10, 2606--2616) and the appearance of an enhanced zone 4.5 and low molecular weight material. 4. Incorporation of zone 4.5 polypeptides into bilayer lipid membranes increases their permeability to D-glucose at 27 and 5 degrees C. 5. It is suggested that the components of the monosaccharide system are present in band 3 polypeptides but that they can undergo proteolysis with some retention of transport activity.
D002352:Carrier Proteins / Q000378:metabolism*; D002463:Cell Membrane Permeability; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008081:Liposomes; D008565:Membrane Proteins / Q000378:metabolism*
D002352:Carrier Proteins; D008081:Liposomes; D008565:Membrane Proteins; D005947:Glucose