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

Bartel, Detlef; Hans, Heidrun; Passow, Hermann

doi:10.1016/0005-2736(89)90427-6

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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: https://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.