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Self-Association of Band 3 Protein from Erythrocyte Membranes in Solutions of a Nonionic Detergent, Ammonyx-Lo

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Pappert,  Gunter
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Schubert,  Dieter
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Pappert, G., & Schubert, D. (1982). Self-Association of Band 3 Protein from Erythrocyte Membranes in Solutions of a Nonionic Detergent, Ammonyx-Lo. In H. Peeters (Ed.), Protides of the Biological Fluids (pp. 117-120). Oxford and New York: Pergamon Pess. doi:10.1016/B978-0-08-027988-6.50028-8.


Cite as: http://hdl.handle.net/21.11116/0000-0008-49E7-2
Abstract
Band 3 protein from human erythrocyte membranes was solubilized and purified, at pH 8, in aqueous solutions of the nonionic detergent Ammonyx-LO. The state of aggregation of the protein was studied by analytical ultracentrifugation and found to be a monomer/dimer/tetramer association equilibrium.