Monomeric erythrocyte band 3 protein transports anions.
The anion transport system of the human erythrocyte membrane was reconstituted in egg phosphatidylcholine membranes by using either the unmodified transport protein, band 3, or covalently crosslinked band 3 dimers. Unilamellar vesicles of a diameter of 32 +/- 3 nm were then isolated from the sample by passage through a French press and subsequent gel filtration. According to sedimentation equilibrium measurements, around 85% of the vesicles were devoid of protein. The remaining 15% contained either a single band 3 monomer or, when crosslinked band 3 protein was used, a single band 3 dimer. Vesicles containing either single monomers or single dimers showed a rapid, inhibitor-sensitive sulfate efflux, and the turnover numbers of band 3 for the inhibitor-sensitive flux component were identical in both systems. This shows that monomeric band 3 protein is able to transport anions and that dimerization of the protein does not change its transport activity.
Lindenthal
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Max-Planck-Institute of Biophysics, Johann Wolfgang Goethe University, Frankfurt am Main, Federal Republic of Germany.
Schubert
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D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure; D001692:Biological Transport; D004910:Erythrocyte Membrane / Q000378:metabolism; D006801:Humans; D046911:Macromolecular Substances; D008433:Mathematics; D008962:Models, Theoretical; D011487:Protein Conformation; D013431:Sulfates / Q000097:blood
D001457:Anion Exchange Protein 1, Erythrocyte; D046911:Macromolecular Substances; D013431:Sulfates