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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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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0007-D4B3-F Versions-Permalink: https://hdl.handle.net/21.11116/0000-0007-D4B4-E
Genre: Zeitschriftenartikel

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 Urheber:
Rudloff, Victor1, Autor           
Lepke, Sigrid1, Autor           
Passow, Hermann1, Autor           
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              

Inhalt

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Schlagwörter: Band 3 protein; Anion transport; 1-Fluoro 2,4-dinitrobenzene; H2DIDS; Erythrocyte
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 1983-09-092001-11-141983-10-31
 Publikationsstatus: Erschienen
 Seiten: 8
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1016/0014-5793(83)81152-1
PMID: 6628684
 Art des Abschluß: -

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Titel: FEBS Letters
  Andere : FEBS Lett.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Amsterdam : Elsevier
Seiten: - Band / Heft: 163 (1) Artikelnummer: - Start- / Endseite: 14 - 21 Identifikator: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501