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Journal Article

The state of association of band 3 protein of the human erythrocyte membrane in solutions of nonionic detergents

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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. (1983). The state of association of band 3 protein of the human erythrocyte membrane in solutions of nonionic detergents. Biochimica et Biophysica Acta-Biomembranes, 730(1), 32-40. doi:10.1016/0005-2736(83)90313-9.


Cite as: https://hdl.handle.net/21.11116/0000-0008-4ABA-4
Abstract
Band 3 protein, the anion transport protein of the human erythrocyte membrane, was solubilized and purified in aqueous solutions of two nonionic detergents: Ammonyx-LO (dimethyl laurylamine oxide) and C12E9 (nonaethylene glycol lauryl ether). The state of association of the purified protein was studied by analytical ultracentrifugation. Band 3 protein solubilized and studied in solutions of Ammonyx-LO was found to be in a monomer/dimer/tetramer association equilibrium. Band 3 protein freshly prepared in C12E9 showed the same behaviour; however, during aging the protein was converted into stable noncovalent dimers. The conversion was retarded by the presence of β-mercaptoethanol or by treatment of the samples with iodoacetamide; it seems to be due to oxidation of the protein by degradation products of the detergent. It is concluded that a monomer/dimer/tetramer association equilibrium is the native state of association of band 3 protein solubilized by nonionic detergents. Since nonionic detergents are assumed not to interfere with protein-protein interactions among membrane proteins, the results strongly support the claim that, in the erythrocyte membrane, band 3 is in a monomer/dimer/tetramer association equilibrium (Dorst, H.-J. and Schubert, D. (1979) Hoppe-Seyler's Z. Physiol. Chem. 360, 1605–1618).