High yield purification of protein 4.1 from human erythrocyte membranes.
Protein 4.1 has been purified from human erythrocyte membranes by a simple method employing the nonionic detergent Tween 20 and anion exchange chromatography. The procedure results in the production of large quantities of protein 4.1, which retains immunoreactivity and the functional properties of binding to spectrin and enhancing the interaction of spectrin and actin.
D000199:Actins / Q000378:metabolism; D001345:Autoradiography; D001798:Blood Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D003598:Cytoskeletal Proteins; D004910:Erythrocyte Membrane / Q000032:analysis*; D006801:Humans; D008565:Membrane Proteins / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D009479:Neuropeptides; D011136:Polysorbates; D011485:Protein Binding; D013049:Spectrin / Q000378:metabolism
D000199:Actins; D001798:Blood Proteins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009479:Neuropeptides; D011136:Polysorbates; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; D013049:Spectrin