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Trypsin digestion for determining orientation of ATPase in Halobacterium saccharovorum membrane vesiclesMembranes prepared by low pressure disruption of cells exhibited no ATPase activity in the absence of Triton X-100, although 43% of the total menadione reductase activity was detected. Trypsin digestion reduced menadione reductase activity by 45% whereas ATPase activity was not affected. Disruption of the membrane fraction at higher pressure solubilized about 45% of the ATPase activity. The soluble activity was still enhanced by Triton X-100, suggesting that the detergent, besides disrupting membrane vesicles, also activated the ATPase. The discrepancy in localization of menadione reductase and ATPase activities raised questions regarding the reliability of using a single marker enzyme as an indicator of vesicle orientation.
Document ID
20040089123
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Kristjansson, H.
(NASA Ames Research Center Moffett Field CA United States)
Hochstein, L. I.
Date Acquired
August 21, 2013
Publication Date
January 1, 1986
Publication Information
Publication: FEMS microbiology letters
Volume: 35
ISSN: 0378-1097
Subject Category
Exobiology
Funding Number(s)
CONTRACT_GRANT: NCA2-OR420-201
Distribution Limits
Public
Copyright
Other
Keywords
NASA Center ARC
NASA Discipline Exobiology

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