Application of a "top-down" approach for the analysis of selective Fe+2 -catalyzed oxidative cleavages of Na.K-ATPase from pig kidney by mass spectrometry. Implication for the energy transduction mechanism

R. Goldshleger*, G. Pachornik, T. Mehlman, M. Benjamin, D. Merhav, S. J.D. Karlish, A. Shainskaya

*Corresponding author for this work

Research output: Contribution to conferencePaperpeer-review

2 Citations (Scopus)

Abstract

The structure-function relations of renal Na/K-ATPase or gastric H,K-ATpase were studied using transition metal (FE or Cu)-catalyzed oxidative cleavage. This technique provides information on the spatial organization in the different conformational states of the important membrane protein. Cleavaged dependent on ATP-Fe2+ reveal positions of Mg2+ in the active site and their changes in different states of the catalytic cycle. MS measurements after electroelution or extraction of hydrophobic proteins from gels, make this a much more powerful technique than hitherto, and should have many other important applications.

Original languageEnglish
Pages103-104
Number of pages2
Publication statusPublished - 2002
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: 2 Jun 20026 Jun 2002

Conference

ConferenceProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Country/TerritoryUnited States
CityOrlando, FL
Period2/6/026/6/02

All Science Journal Classification (ASJC) codes

  • Spectroscopy

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