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  The binding of Ca2+ to solubilized band 3 protein of the human erythrocyte membrane

Passing, R., & Schubert, D. (1983). The binding of Ca2+ to solubilized band 3 protein of the human erythrocyte membrane. Hoppe-Seyler's Zeitschrift für physiologische Chemie, 354(7), 873-878. doi:10.1515/bchm2.1983.364.2.873.

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 Urheber:
Passing, Reinhard1, Autor           
Schubert, Dieter1, Autor           
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              

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 Zusammenfassung: The binding of 45Ca2+ to isolated band 3 protein, the anion transport protein of the human erythrocyte membrane, was studied by equilibrium dialysis. The protein was solubilized and purified by either the nonionic detergent Ammonyx-L0 or acetic acid. Each preparation of band 3 protein showed a single high-affinity Ca2+ binding site and several Ca2+ binding sites of lower affinity. The association constant of the high-affinity site was 4-13 X 104M-1; it was only moderately dependent on ionic strength. Mg2+ effectively competed with Ca2+ for the site. Anion exchange across the human erythrocyte membrane is inhibited by micromolar concentrations of intracellular Ca2+. Our results suggest that this inhibition is due to the binding of the cation to a single site on band 3 protein.

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Sprache(n): eng - English
 Datum: 1983-03-301983-07-01
 Publikationsstatus: Erschienen
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1515/bchm2.1983.364.2.873
PMID: 6618447
 Art des Abschluß: -

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Titel: Hoppe-Seyler's Zeitschrift für physiologische Chemie
  Kurztitel : Biol. Chem. Hoppe-Seyler
  Andere : Biological Chemistry Hoppe-Seyler
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Berlin : W. de Gruyter
Seiten: - Band / Heft: 354 (7) Artikelnummer: - Start- / Endseite: 873 - 878 Identifikator: ISSN: 0177-3593
CoNE: https://pure.mpg.de/cone/journals/resource/954925623257