Identification and properties of the glucose transporter of human erythrocytes.
Several lines of studies were undertaken to clarify the identity of the glucose transporter of human erythrocytes. Peptide maps of zone 4.5 which is the main component of the purified transporter fraction, were different from those of band 3. Cytochalasin B bound to the purified transporter fraction but not to band 3. Antibody raised against the purified transporter fraction cross-reacted with zone 4.5 and moderately with band 7, but not with other erythrocyte membrane proteins. These results indicate that zone 4.5 is the transporter (or a part of the transporter) and is not a fragment of band 3. With ferritin antibody electron microscopy and freeze-fracture electron microscopy, the glucose transporter were found to evenly distributed in reconstituted liposomes. Further morphological analysis coupled with transport assays showed the distribution of the transporters was random and was satisfactorily fitted to Poisson distribution, indicating reversible association of the transporters does not occur in liposomes and is not necessary for transport activity. This communication summarises our recent studies on identification and properties of the glucose transporter of human erythrocytes. A full account of the studies is published elsewhere (22, 23).
D001786:Blood Glucose / Q000378:metabolism*; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000648:ultrastructure; D004912:Erythrocytes / Q000378:metabolism*; D005614:Freeze Fracturing; D006801:Humans; D008081:Liposomes; D008563:Membrane Lipids / Q000097:blood; D008854:Microscopy, Electron; D009004:Monosaccharide Transport Proteins; D010446:Peptide Fragments / Q000032:analysis
D001786:Blood Glucose; D002352:Carrier Proteins; D008081:Liposomes; D008563:Membrane Lipids; D009004:Monosaccharide Transport Proteins; D010446:Peptide Fragments