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 language | English |
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| Pages | 103-104 |
| Number of pages | 2 |
| Publication status | Published - 2002 |
| Event | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: 2 Jun 2002 → 6 Jun 2002 |
Conference
| Conference | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics |
|---|---|
| Country/Territory | United States |
| City | Orlando, FL |
| Period | 2/6/02 → 6/6/02 |
All Science Journal Classification (ASJC) codes
- Spectroscopy