Nucleotide-Protectable Labeling of Sulfhydryl Groups in Subunit I of the ATPhase from Halobacterium Saccharovorum
- Hochstein, Lawrence I.
- Jul. 1992.
- Physical Description:
- 1 electronic document
- Additional Creators:
- Sulzner, Michael and Stan-Lotter, Helga
- hdl.handle.net , Connect to this object online.
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- A membrane-bound ATPase from the archaebacterium Halobacterium saccharovorum is inhibited by N-ethyl-maleimide in a nucleotide-protectable manner. When the enzyme was incubated with N-[C-14]jethylmaleimide, the bulk of radioactivity was as- sociated with the 87,000-Da subunit (subunit 1). ATP, ADP, or AMP reduced incorporation of the inhibitor. No charge shift of subunit I was detected following labeling with N-ethylmaleimide, indicating an electroneutral reaction. The results are consistent with the selective modification of sulfhydryl groups in subunit I at or near the catalytic site and are further evidence of a resemblance between this archaebacterial ATPase and the vacuolar-type ATPases.
- Other Subject(s):
- NASA Technical Reports Server (NTRS) Collection.
- Document ID: 19980008069.
Archives of Biochemistry and Biophysics(ISSN 0003-9861); Volume 296; No. 1; 347-349.
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