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PMID: 6097317 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Saturation of the internal sodium site of the sodium pump can distort estimates of potassium affinity.

Biophysical journal ·Vol. 46 ·No. 6 ·1984-12-00 ·Pages 719-27

Cohen I, Falk R, Gintant G

Abstract

The Na+/K+ exchange pump in cardiac Purkinje strands has been well studied with the voltage clamp and Na+-selective microelectrodes. Models describing the observed results suggest that the pump rate can be considered proportional to [Na+]i over the range examined and depends on external [K+] in accordance with Michaelis-Menten kinetics. Estimates of the external [K+] that achieves a half-maximal pump rate (Km) range from 0.9 to 6.3 mM depending on the preparation and method of estimation. Here we show that much of the variability in the estimates of the Km can be eliminated when saturation of the internal Na+ pump site is taken into account. If the half-activation concentration for saturation of this Na+ site is sufficiently high (greater than 20 mM), removal of intracellular Na+ in response to a Na+ load will approximate first-order kinetics. Under these conditions however, Na+ saturation will nevertheless cause large systematic errors in estimates of the K+ dependence of pump activity.

MeSH Terms
Animals Heart Conduction System/metabolism Kinetics Mathematics Models, Biological Potassium/metabolism Purkinje Fibers/metabolism Sodium/metabolism Sodium-Potassium-Exchanging ATPase/metabolism
Chemicals
Sodium Sodium-Potassium-Exchanging ATPase Potassium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Cohen I
Falk R
Gintant G
References (28)
28 references, click to expand
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1984-12-00
Pages
719-27
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1435109
Subset
IM
Grants
NHLBI NIH HHS · HL20558 · United States
NHLBI NIH HHS · HL28958 · United States
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