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

Rudloff, Victor; Lepke, Sigrid; Passow, Hermann

doi:10.1016/0014-5793(83)81152-1

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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

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.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0007-D4B3-F Version Permalink: https://hdl.handle.net/21.11116/0000-0007-D4B4-E

Genre: Journal Article

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Creators:
Rudloff, Victor¹, Author
Lepke, Sigrid¹, Author
Passow, Hermann¹, Author

Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817

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Free keywords: Band 3 protein; Anion transport; 1-Fluoro 2,4-dinitrobenzene; H₂DIDS; Erythrocyte

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.

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Language(s): eng - English

Dates: Submitted: 1983-09-09Published Online: 2001-11-14Date issued: 1983-10-31

Publication Status: Issued

Pages: 8

Publishing info: -

Table of Contents: -

Rev. Type: Peer

Identifiers: DOI: 10.1016/0014-5793(83)81152-1
PMID: 6628684

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Title: FEBS Letters

Other : FEBS Lett.

Source Genre: Journal

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Publ. Info: Amsterdam : Elsevier

Pages: - Volume / Issue: 163 (1) Sequence Number: - Start / End Page: 14 - 21 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501