English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Two-electrode voltage-clamp analysis of Na,K-ATPase asparagine 776 mutants

Koenderink, J. B., Geibel, S., Grabsch, E., De Pont, J. J. H., Bamberg, E., & Friedrich, T. (2003). Two-electrode voltage-clamp analysis of Na,K-ATPase asparagine 776 mutants. Annals of the New York Academy of Sciences, 986, 150-154. doi:10.1111/j.1749-6632.2003.tb07152.x.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Koenderink, Jan B.1, Author           
Geibel, Sven1, Author           
Grabsch, Eva1, Author           
De Pont, Jan Joep H.H.M.2, Author
Bamberg, Ernst1, Author           
Friedrich, Thomas1, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Department of Biochemistry, Nijmegen Center for Molecular Life Sciences, Nijmegen, The Netherlands, ou_persistent22              

Content

show
hide
Free keywords: Xenopus laevis; electrophysiology; transient currents; Asn776; mutagenesis
 Abstract: Steady-state and pre-steady-state currents of Asn776 mutants of Na,K-ATPase are presented. The stationary current generated by N776Q strongly depends on the membrane potential, but has a negative slope, opposite to that of the wild-type enzyme. The apparent rate constant of the reaction sequence E1P(Na+) <--> E2P + Na+ of this mutant is rather independent of the membrane potential and is at resting and depolarizing membrane potential higher than that of the wild-type enzyme. Thus, the voltage-dependent increase of the rate coefficient of the wild type that is associated with extracellular Na+ rebinding is almost absent in the N776Q mutant. These findings indicate that dislocating the carboxamide group of Asn776 decreases the affinity of sodium at its extracellular binding site.

Details

show
hide
Language(s): eng - English
 Dates: 2006-01-242003-04-01
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Annals of the New York Academy of Sciences
  Other : Ann. N.Y. Acad. Sci.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: New York : New York Academy of Sciences
Pages: - Volume / Issue: 986 Sequence Number: - Start / End Page: 150 - 154 Identifier: ISSN: 0077-8923
CoNE: https://pure.mpg.de/cone/journals/resource/954926958894_2