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Mikael Esmann

The Na,K-ATPase

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

The Na,K-ATPase. / Skou, J C; Esmann, Mikael.

I: Journal of Bioenergetics and Biomembranes, Bind 24, Nr. 3, 01.06.1992, s. 249-261.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Skou, JC & Esmann, M 1992, 'The Na,K-ATPase', Journal of Bioenergetics and Biomembranes, bind 24, nr. 3, s. 249-261.

APA

Skou, J. C., & Esmann, M. (1992). The Na,K-ATPase. Journal of Bioenergetics and Biomembranes, 24(3), 249-261.

CBE

Skou JC, Esmann M. 1992. The Na,K-ATPase. Journal of Bioenergetics and Biomembranes. 24(3):249-261.

MLA

Skou, J C og Mikael Esmann. "The Na,K-ATPase". Journal of Bioenergetics and Biomembranes. 1992, 24(3). 249-261.

Vancouver

Skou JC, Esmann M. The Na,K-ATPase. Journal of Bioenergetics and Biomembranes. 1992 jun 1;24(3):249-261.

Author

Skou, J C ; Esmann, Mikael. / The Na,K-ATPase. I: Journal of Bioenergetics and Biomembranes. 1992 ; Bind 24, Nr. 3. s. 249-261.

Bibtex

@article{88e3ab9b48a840d5b6d7746326f0c7b3,
title = "The Na,K-ATPase",
abstract = "The energy dependent exchange of cytoplasmic Na+ for extracellular K+ in mammalian cells is due to a membrane bound enzyme system, the Na,K-ATPase. The exchange sustains a gradient for Na+ into and for K+ out of the cell, and this is used as an energy source for creation of the membrane potential, for its de- and repolarisation, for regulation of cytoplasmic ionic composition and for transepithelial transport. The Na,K-ATPase consists of two membrane spanning polypeptides, an alpha-subunit of 112-kD and a beta-subunit, which is a glycoprotein of 35-kD. The catalytic properties are associated with the alpha-subunit, which has the binding domain for ATP and the cations. In the review, attention will be given to the biochemical characterization of the reaction mechanism underlying the coupling between hydrolysis of the substate ATP and transport of Na+ and K+.",
keywords = "Adenosine Triphosphate, Animals, Binding Sites, Cell Membrane, Potassium, Protein Conformation, Sodium, Sodium-Potassium-Exchanging ATPase",
author = "Skou, {J C} and Mikael Esmann",
year = "1992",
month = "6",
day = "1",
language = "English",
volume = "24",
pages = "249--261",
journal = "Journal of Bioenergetics and Biomembranes",
issn = "0145-479X",
publisher = "Springer",
number = "3",

}

RIS

TY - JOUR

T1 - The Na,K-ATPase

AU - Skou, J C

AU - Esmann, Mikael

PY - 1992/6/1

Y1 - 1992/6/1

N2 - The energy dependent exchange of cytoplasmic Na+ for extracellular K+ in mammalian cells is due to a membrane bound enzyme system, the Na,K-ATPase. The exchange sustains a gradient for Na+ into and for K+ out of the cell, and this is used as an energy source for creation of the membrane potential, for its de- and repolarisation, for regulation of cytoplasmic ionic composition and for transepithelial transport. The Na,K-ATPase consists of two membrane spanning polypeptides, an alpha-subunit of 112-kD and a beta-subunit, which is a glycoprotein of 35-kD. The catalytic properties are associated with the alpha-subunit, which has the binding domain for ATP and the cations. In the review, attention will be given to the biochemical characterization of the reaction mechanism underlying the coupling between hydrolysis of the substate ATP and transport of Na+ and K+.

AB - The energy dependent exchange of cytoplasmic Na+ for extracellular K+ in mammalian cells is due to a membrane bound enzyme system, the Na,K-ATPase. The exchange sustains a gradient for Na+ into and for K+ out of the cell, and this is used as an energy source for creation of the membrane potential, for its de- and repolarisation, for regulation of cytoplasmic ionic composition and for transepithelial transport. The Na,K-ATPase consists of two membrane spanning polypeptides, an alpha-subunit of 112-kD and a beta-subunit, which is a glycoprotein of 35-kD. The catalytic properties are associated with the alpha-subunit, which has the binding domain for ATP and the cations. In the review, attention will be given to the biochemical characterization of the reaction mechanism underlying the coupling between hydrolysis of the substate ATP and transport of Na+ and K+.

KW - Adenosine Triphosphate

KW - Animals

KW - Binding Sites

KW - Cell Membrane

KW - Potassium

KW - Protein Conformation

KW - Sodium

KW - Sodium-Potassium-Exchanging ATPase

M3 - Journal article

C2 - 1328174

VL - 24

SP - 249

EP - 261

JO - Journal of Bioenergetics and Biomembranes

JF - Journal of Bioenergetics and Biomembranes

SN - 0145-479X

IS - 3

ER -