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Halobacterial adenosine triphosphatases and the adenosine triphosphatase from Halobacterium saccharovorumMembranes prepared from various members of the genus Halobacterium contained a Triton X-l00 activated adenosine triphosphatase. The enzyme from Halobacterium saccharovorum was unstable in solutions of low ionic strength and maximally active in the presence of 3.5 M NaCl. A variety of nucleotide triphosphates was hydrolyzed. MgADP, the product of ATP hydrolysis, was not hydrolyzed and was a competitive inhibitor with respect to MgATP. The enzyme from H. saccharovorum was composed of at least 2 and possibly 4 subunits. The 83-kDa and 60-kDa subunits represented about 90 percent of total protein. The 60-kDa subunit reacted with dicyclohexyl-carbodiimide when inhibition was carried out in an acidic medium. The enzyme from H. saccharovorum, possesses properties of an F(1)F(0) as well as an E(1)E(2) ATPase.
Document ID
19870040125
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Kristjansson, Hordur
(NASA Ames Research Center Moffett Field, CA, United States)
Sadler, Martha H.
(NASA Ames Research Center Moffett Field, CA, United States)
Hochstein, Lawrence I.
(NASA Ames Research Center Moffett Field, CA, United States)
Date Acquired
August 13, 2013
Publication Date
January 1, 1986
Publication Information
Publication: FEMS Microbiology Reviews
Volume: 39
ISSN: 0168-6445
Subject Category
Life Sciences (General)
Accession Number
87A27399
Distribution Limits
Public
Copyright
Other

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