The human erythrocyte nucleoside and glucose transporters are both band 4.5 membrane polypeptides.
Human erythrocyte membranes and partially purified nucleoside transporter (band 4.5 and 7) were photoaffinity labelled with 3H-labelled 6-[(4-nitrobenzyl)thio]-9-beta-D-ribofuranosylpurine under equilibrium binding conditions. Band 4.5 was the major site of radiolabelling in both preparations. These experiments provide additional evidence to implicate band 4.5 polypeptides in nucleoside permeation, proteins previously shown to be involved in hexose transport.
D000345:Affinity Labels / Q000494:pharmacology; D001692:Biological Transport / Q000187:drug effects; D001786:Blood Glucose / Q000378:metabolism*; D002352:Carrier Proteins / Q000097:blood*; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000097:blood*; D009004:Monosaccharide Transport Proteins; D009705:Nucleosides / Q000097:blood*; D013868:Thioinosine / Q000031:analogs & derivatives / Q000494:pharmacology
D000345:Affinity Labels; D001786:Blood Glucose; D002352:Carrier Proteins; D008565:Membrane Proteins; D009004:Monosaccharide Transport Proteins; D009705:Nucleosides; D013868:Thioinosine; C001789:4-nitrobenzylthioinosine