Characterization and identification of the glucose transporter of human erythrocytes.
The glucose transporter was purified from human erythrocytes (Kasahara, M. and Hinkle, P.C. (1977) J. Biol. Chem. 252, 7384-7390). The following results support the conclusion that a major protein in the purified transporter fraction, zone 4.5 is the glucose transporter (or a part of the transporter) and is different from band 3: (1) peptide maps of zone 4.5 were similar throughout the broad band in sodium dodecyl sulfate-gel electrophoresis and were different from those of band 3, (2) specific binding of cytochalasin B was found to the transporter fraction, but not to a band 3 fraction, (3) the N-terminal amino acid analysis of the transporter fraction showed a single N-terminal of lysine, whereas the band 3 fraction showed no clear N-terminal, and (4) the rabbit antibody raised against the transporter fraction formed a precipitation line with the transporter fraction, but not with the band 3 fraction. A filtration apparatus was devised for quick and accurate measurement of cytochalasin B binding, with which results comparable to those from equilibrium dialysis were obtained.
D001786:Blood Glucose / Q000378:metabolism*; D002352:Carrier Proteins / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D000939:Epitopes / Q000032:analysis; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D005779:Immunodiffusion; D008081:Liposomes; D008565:Membrane Proteins / Q000097:blood / Q000302:isolation & purification; D009004:Monosaccharide Transport Proteins; D010446:Peptide Fragments / Q000032:analysis
D001786:Blood Glucose; D002352:Carrier Proteins; D000939:Epitopes; D008081:Liposomes; D008565:Membrane Proteins; D009004:Monosaccharide Transport Proteins; D010446:Peptide Fragments