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Journal Article

Towards the localization of the essential arginine residues in the band 3 protein of human red blood cell membranes

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Böhm,  Roger
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Zaki,  Laila
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Böhm, R., & Zaki, L. (1996). Towards the localization of the essential arginine residues in the band 3 protein of human red blood cell membranes. Biochimica et Biophysica Acta-Biomembranes, 1280(2), 238-242. doi:10.1016/0005-2736(95)00303-7.


Cite as: https://hdl.handle.net/21.11116/0000-0007-5C7E-6
Abstract
The effects of 4-hydroxy-3-nitrophenylglyoxal (HNPG), on the binding of eosin-5-maleimide (EMA), and diethyl pyrocarbonate (DEPC) to the anion transport system in the human red blood cell membrane, have been investigated. HNPG is a reversibly binding, arginine-specific, anion transport competitive inhibitor, known to act on the anion binding site. The EMA reaction site is an external facing lysine residue (Lys-430) in the 17 kDa transmembrane segment. The DEPC reaction site is an intracellular histidine (His-819) in the 35 kDa fragment. The results show that inhibition of the transport system with EMA increases in presence of HNPG to about 2.3 times. This finding suggests a positive cooperativity between the HNPG and EMA binding site and give evidence that the essential arginine is either nearby or allosterically linked to Lys-430. The inhibition of the cells with DEPC was nearly unchanged or slightly decreased in the presence of 10 mM HNPG. These results suggest that the intracellular His-residue which reacts with DEPC is not a part of the transport pathway. Our experiments with 4,4′-dinitrostilbene-2,2′-disulfonate (DNDS) have shown that its affinity to the transport system does not change after pre-treatment with phenylglyoxal (PG). We also found that the binding of [14C]phenylglyoxal (PG) to band 3 reduces significantly in presence of chloride. This is another evidence for the direct involvement of arginine residues in substrate binding.