The isolation of human-erythrocyte band-3 polypeptide labelled with a photosensitive hydrophobic probe.
To investigate the intramembranous domains of the major band-3 polypeptide, human erythrocyte membranes were labelled with 1-azido-4-[125I]iodobenzene. The anion-exchange protein has been isolated by a new procedure that decreases possible contamination by other integral membrane proteins of similar molecular weight. After chemical modification, the protein was subjected to proteolytic cleavage by several proteinases to yield a distinct pattern of peptides, a few of which contained radioactivity.
D001457:Anion Exchange Protein 1, Erythrocyte / Q000302:isolation & purification*; D001386:Azides; D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D004591:Electrophoresis, Polyacrylamide Gel; D004592:Electrophoresis, Starch Gel; D004910:Erythrocyte Membrane / Q000032:analysis*; D006801:Humans; D007202:Indicators and Reagents; D007457:Iodine Radioisotopes; D010446:Peptide Fragments / Q000032:analysis; D010777:Photochemistry
D001457:Anion Exchange Protein 1, Erythrocyte; D001386:Azides; D007202:Indicators and Reagents; D007457:Iodine Radioisotopes; D010446:Peptide Fragments; C020866:1-azido-4-iodobenzene