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Identification by site-directed mutagenesis of Lys-558 as the covalent attachment site of H2DIDS in the mouse erythroid band 3 protein

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Bartel,  Detlef
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Hans,  Heidrun
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Passow,  Hermann
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Bartel, D., Hans, H., & Passow, H. (1989). Identification by site-directed mutagenesis of Lys-558 as the covalent attachment site of H2DIDS in the mouse erythroid band 3 protein. Biochimica et Biophysica Acta-Biomembranes, 985(3), 355-358. doi:10.1016/0005-2736(89)90427-6.


Cite as: http://hdl.handle.net/21.11116/0000-0007-CD4A-0
Abstract
After functional expression of mouse erythroid band 3 by cRNA microinjection into Xenopus oocytes, 36Cl efflux is irreversibly inhibited by H2DIDS. When a cRNA is injected that is derived from a cDNA in which the nucleotides encoding for lysine-558 were replaced by nucleotides encoding for asparagine, transport and inhibition of transport by H2DIDS still occur. However, when measured under conditions where no intramolecular crosslinking takes place the inhibition by H2DIDS is no longer irreversible. This indicates that thiourea bond formation between H2DIDS and band 3 takes place at Lys-558.