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  Investigation of charge translocation by ion pumps and carriers using caged substrates

Fendler, K., Hartung, K., Nagel, G., & Bamberg, E. (1998). Investigation of charge translocation by ion pumps and carriers using caged substrates. In G. Marriott (Ed.), Methods in Enzymology (pp. 289-306). Academic Press. doi:10.1016/S0076-6879(98)91020-5.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0007-A5B3-4 Version Permalink: https://hdl.handle.net/21.11116/0000-0007-A5B4-3
Genre: Book Chapter

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 Creators:
Fendler, Klaus1, Author           
Hartung, Klaus1, Author           
Nagel, Georg1, Author           
Bamberg, Ernst1, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              

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 Abstract: Publisher Summary:
This chapter presents studies on the application of caged compounds to planar lipid membranes as well as on giant patches of heart cell membranes. The chapter gives a few examples of transport ATPases and carriers that have been investigated using caged substrates. The advantage of this approach is the high time resolution that allows the investigation of pre steady-state kinetics. A number of other ion-translocating ATPases are investigated in the chapter using caged ATP: the Ca-ATPase from sarcoplasmatic reticulum, the H,K-ATPase from stomach, the F0F1-ATPase from chloroplasts, and the Kdp-ATPase from the plasma membrane of Escherichia coli. In the case of caged ATP the time resolution is limited by the time constant of ATP release from the caged compound used in those studies. By working at a somewhat acidic pH (6.2), ATP is released rapidly enough to study most of the enzymatic reactions of interest.

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Language(s): eng - English
 Dates: 2004-01-071998
 Publication Status: Issued
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0076-6879(98)91020-5
 Degree: -

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Title: Methods in Enzymology
  Subtitle : Caged Compounds
Source Genre: Series
 Creator(s):
Marriott, Gerard , Editor
Affiliations:
-
Publ. Info: Academic Press
Pages: 529 Volume / Issue: 291 Sequence Number: - Start / End Page: 289 - 306 Identifier: ISBN: 978-0-12-182192-0
ISSN: 0076-6879