Publikation:

(Na + K )-ATPase in artificial lipid vesicles : influence of lipid structure on pumping rate

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NaK_ATPase_in_artificial_lipid_vesicles.pdf
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Datum

1986

Autor:innen

Marcus, Madeleine M.
Schwendener, Rico
Weder, H.-G.
Läuger, Peter

Herausgeber:innen

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URI (zitierfähiger Link)
http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-39494
DOI (zitierfähiger Link)
https://doi.org/10.1016/0005-2736(86)90120-3
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Internationale Patentnummer

Link zur Lizenz
Attribution-NonCommercial-NoDerivs 2.0 Generic

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Open Access-Veröffentlichung
Open Access Green

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Biologie: Publikationen
Core Facility der Universität Konstanz

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Titel in einer weiteren Sprache

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Published

Erschienen in

Biochimica et Biophysica Acta - Biomembranes. 1986, 854(2), pp. 270-278. ISSN 0005-2736. Available under: doi: 10.1016/0005-2736(86)90120-3

Zusammenfassung

(Na+K)-ATPase from kidney outer medulla was incorporated into tightly-sealed, single-shelled lipid vesicles by a detergent-dialysis procedure. The rate of ATP-driven potassium extrusion from vesicles formed from different phosphatidylcholines (PC) was measured optically, using a voltage-sensitive dye in the presence of valinomycin. High transport rates were observed for di(18: l)PC, di(20: l)PC and di(22: l)pC, whereas vesicles formed from di(14: l)PC and di(16: l)PC were virtually inactive. The variation of pumping activity with lipid structure mainly results from differences in the amount of enzyme incorporated with the correct orientation into the vesicle membrane, and to a lesser extent from lipid-dependent variations of the intrinsic turnover rate of the enzyme. The activation energy of ion transport decreases in the order di(16: l)pC, di(18: l)pC, di(20: l)pC = di(22: 1)pC.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

(Na+K)-ATPase, Membrane reconstitution, Lipid-protein interaction, Pumping activity, (Rabbit kidney)

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ISO 690MARCUS, Madeleine M., Hans-Jürgen APELL, Milena ROUDNA, Rico SCHWENDENER, H.-G. WEDER, Peter LÄUGER, 1986. (Na + K )-ATPase in artificial lipid vesicles : influence of lipid structure on pumping rate. In: Biochimica et Biophysica Acta - Biomembranes. 1986, 854(2), pp. 270-278. ISSN 0005-2736. Available under: doi: 10.1016/0005-2736(86)90120-3
BibTex
@article{Marcus1986ATPas-8405,
  year={1986},
  doi={10.1016/0005-2736(86)90120-3},
  title={(Na + K )-ATPase in artificial lipid vesicles : influence of lipid structure on pumping rate},
  number={2},
  volume={854},
  issn={0005-2736},
  journal={Biochimica et Biophysica Acta - Biomembranes},
  pages={270--278},
  author={Marcus, Madeleine M. and Apell, Hans-Jürgen and Roudna, Milena and Schwendener, Rico and Weder, H.-G. and Läuger, Peter}
}
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    <dcterms:abstract xml:lang="eng">(Na+K)-ATPase from kidney outer medulla was incorporated into tightly-sealed, single-shelled lipid vesicles by a detergent-dialysis procedure. The rate of ATP-driven potassium extrusion from vesicles formed from different phosphatidylcholines (PC) was measured optically, using a voltage-sensitive dye in the presence of valinomycin. High transport rates were observed for di(18: l)PC, di(20: l)PC and di(22: l)pC, whereas vesicles formed from di(14: l)PC and di(16: l)PC were virtually inactive. The variation of pumping activity with lipid structure mainly results from differences in the amount of enzyme incorporated with the correct orientation into the vesicle membrane, and to a lesser extent from lipid-dependent variations of the intrinsic turnover rate of the enzyme. The activation energy of ion transport decreases in the order di(16: l)pC, di(18: l)pC, di(20: l)pC = di(22: 1)pC.</dcterms:abstract>
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