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- W2030575563 abstract "Abstract The F1-ATPase from Mycobacterium phlei is inactivated by dicyclohexylcarbodiimide (DCCD), 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl) and quinacrine mustard. The inactivation is both time-and concentration-dependent and in the case of DCCD being more pronounced at acidic pH. The minimum inactivation half-time ( t 1 2 ) for DCCD, NBD-Cl and quinacrine mustard was observed to be 14, 6 and 7 min, respectively. Inactivation of F1-ATPase resulted in the incorporation of [14C]DCCD as well as [14C]NBD-Cl into α and γ subunits. The incorporation of label into α and γ subunits, utilizing [14C]NBD-Cl, was reversible by dithiothreitol. Complete inactivation, by linear extrapolation to zero activity, revealed that 4 mol [14C]DCCD and 4 mol [14C]NBD-Cl bind per mol F1-ATPase. Kinetic and binding studies show that these probes bind to site(s) distinct from ATP-binding site in F1-ATPase from M. phlei." @default.
- W2030575563 created "2016-06-24" @default.
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- W2030575563 date "1984-01-01" @default.
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- W2030575563 title "Inactivation and the site of labeling of F1-ATPase from Mycobacterium phlei by dicyclohexylcarbodiimide, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole and quinacrine mustard" @default.
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- W2030575563 doi "https://doi.org/10.1016/0005-2728(84)90146-4" @default.
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