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  Modulation of the Ca2+- or Pb2+-activated K+-selective channels in human red cells. II. Parallelisms to modulation of the activity of a membrane-bound oxidoreductase

Fehlau, R., Grygorczyk, R., Fuhrmann, G., & Schwarz, W. (1989). Modulation of the Ca2+- or Pb2+-activated K+-selective channels in human red cells. II. Parallelisms to modulation of the activity of a membrane-bound oxidoreductase. Biochimica et Biophysica Acta-Biomembranes, 978(1), 37-42. doi:10.1016/0005-2736(89)90495-1.

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 Urheber:
Fehlau, R.1, Autor
Grygorczyk, Ryszard2, Autor           
Fuhrmann, G.F.1, Autor
Schwarz, Wolfgang2, Autor           
Affiliations:
1Institut für Pharmakologie und Toxikologie, Universität Marburg, Germany, ou_persistent22              
2Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              

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Schlagwörter: Calcium activated potassium channel; Potassium ion channel; Atebrin; Menadione; Oxidoreductase; Lead; (Human erythrocyte)
 Zusammenfassung: Modulation of Ca2+-activable K+ permeability was compared with modulation of a membrane-bound oxidoreductase activity in human erythrocytes. Changes in the K+ permeability were monitored by flux measurements and single-channel recordings. The enzyme activity was detected by measuring reduction of ferricyanide. Pb2+, Atebrin and menadione had parallel effects on the channel protein and the enzyme. In contrast, propranolol stimulates K+ permeability, but is without effect on enzyme activity. The results demonstrate that the K+ channel and the enzyme are distinct membrane proteins but that the enzyme activity may influence channel gating.

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Sprache(n): eng - English
 Datum: 1988-06-272003-03-311989-01-16
 Publikationsstatus: Erschienen
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1016/0005-2736(89)90495-1
PMID: 2914129
 Art des Abschluß: -

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Titel: Biochimica et Biophysica Acta-Biomembranes
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Amsterdam : Elsevier
Seiten: - Band / Heft: 978 (1) Artikelnummer: - Start- / Endseite: 37 - 42 Identifikator: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702