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Inhibition of anion transport across the red cell membrane by dinitrophenylation of a specific lysine residue at the H2DIDS binding site of the band 3 protein

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Rudloff,  Victor
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Lepke,  Sigrid
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

Rudloff, V., Lepke, S., & Passow, H. (1983). Inhibition of anion transport across the red cell membrane by dinitrophenylation of a specific lysine residue at the H2DIDS binding site of the band 3 protein. FEBS Letters, 163(1), 14-21. doi:10.1016/0014-5793(83)81152-1.


Cite as: http://hdl.handle.net/21.11116/0000-0007-D4B3-F
Abstract
The inhibition of anion transport by dinitrophenylation of the red cell membrane is brought about by the modification of a single lysine residue located on the 17-kDa segment of the band 3 protein. This residue is identical with Lys a, which is also capable of reacting with one of the two isothiocyanate groups of 4,4'-diisothiocyano dihydro-stilbene-2,2'-disulfonate (H2DIDS). The rate of reaction between Lys a and 1-fluoro-2,4-dinitrobenzene is reduced when a second lysine residue on the 35-kDa segment of the band 3 protein becomes dinitrophenylated. This latter residue is not identical with Lys b which is known to be present on the 35-kDa segment and involved in the cross-linking of this segment with the 17-kDa segment by H2DIDS.