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- W2144614246 abstract "A membrane-bound ATPase from the archaebacterium Halobacterium saccharovorum is inhibited by N-ethylmaleimide in a nucleotide-protectable manner (Stan-Lotter et al., 1991, Arch. Biochem. Biophys. 284, 116-119). When the enzyme was incubated with N-[14C]ethylmaleimide, the bulk of radioactivity was associated with the 87,000-Da subunit (subunit I). 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." @default.
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- W2144614246 date "1992-07-01" @default.
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- W2144614246 title "Nucleotide-protectable labeling of sulfhydryl groups in subunit I of the ATPase from Halobacterium saccharovorum" @default.
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- W2144614246 doi "https://doi.org/10.1016/0003-9861(92)90582-h" @default.
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