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on archaebacterial atpase from halobacterium saccharovorumThe energy transducing ATPase from Halobacterium saccharovorum was studied in order to define the origin of energy transducing systems. The ATPase required high salt concentration (4M NaCl) for activity; activity was rapidly lost when NaCl was below 1 Molar. At low salt concentration, the membrane bound ATPase activity could be stabilized in presence of spermine. However, following solubilization spermine was ineffective. Furthermore, F1 ATPase activity was stabilized by ammonium sulfate even when the NaCl concentration was less than 1 Molar. These studies suggest that stabilization by hydrophobic interactions preceded ionic ones in the evolution of the energy transducing ATPases.
Document ID
19840057721
Document Type
Reprint (Version printed in journal)
Authors
Kristjansson, H.
(Maryland Univ. College Park, MD, United States)
Ponnamperuma, C.
(Maryland, University College Park, MD, United States)
Hochstein, L.
(NASA Ames Research Center Extraterrestrial Research Div., Moffett Field, CA, United States)
Altekar, W.
(Maryland Univ. College Park, MD, United States)
Date Acquired
August 12, 2013
Publication Date
January 1, 1984
Publication Information
Publication: Origins of Life
Volume: 14
Issue: 1-4,
ISSN: 0302-1688
Subject Category
LIFE SCIENCES (GENERAL)
Distribution Limits
Public
Copyright
Other