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Purification and properties of an ATPase from Sulfolobus solfataricusThe paper reports properties of a sulfite-activated ATPase from Sulfolobus solfataricus, purified using ammonium sulfate precipitation, column chromatography on UltraGel and Sepharose 6B, and SDS-PAGE. The 92-fold purified enzyme had a relative molecular mass of 370,000. It could be dissociated into three subunits with respective molecular masses of 63,000, 48,000, and 24,000. The ATPase activity was found to be inhibitable by nitrate, N-ethylmaleimide (which bound predominantly to the largest subunit), and 4-chloro 7-nitrobenzofurazan, but not by azide, quercetin, or vanadate. While the ATPase from S. solfataricus shared a number of properties with the S. acidocaldarius ATPase, there were also significant differences suggesting the existence of several types of archaeal ATPases.
Document ID
19930048118
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Hochstein, Lawrence I.
(NASA Ames Research Center Moffett Field, CA, United States)
Stan-Lotter, Helga
(NASA Ames Research Center Moffett Field; SETI Inst., Mountain View, CA, United States)
Date Acquired
August 16, 2013
Publication Date
May 15, 1992
Publication Information
Publication: Archives of Biochemistry and Biophysics
Volume: 295
Issue: 1
ISSN: 0003-9861
Subject Category
Life Sciences (General)
Accession Number
93A32115
Funding Number(s)
CONTRACT_GRANT: NCC2-578
Distribution Limits
Public
Copyright
Other

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