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GR is a 108-kDa, homodimeric flavoenzyme that catalyzes the [beta]-nicotinamide-adenine dinucleotide phosphate (NADPH)-dependent reduction of oxidized glutathione (GSSG) to its reduced form (GSH), thus participating in cellular defense mechanisms against oxidative stress
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Inactivation-reactivation of two-electron reduced Escherichia coli glutathione reductase involving a dimer-monomer equilibrium
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Further and more detailed insights in the mechanisms of how aggregation affects properties of the unfolded state can be gained from studies where aggregation, in particular of thermal unfolded states, is suppressed
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The dependence of the ANS fluorescence intensity, in ice at - 13°C, on the starting ANS concentration in solution (10-200 µM) is shown in Fig
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Such a link between the instability to freeze-thawing and propensity to bind ANS in ice supports the notion that irreversible damage to freeze labile proteins, often resulting in enzyme inactivation and or protein aggregation, is likely to have originated from partial unfolding of the globular structure in ice
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The large bandwidth, in turn, requires a large magnetic field gradient
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This is achieved by a component in the flux that, after the solvent has evaporated and the solids of the flux are molten, forms a continuous film over the surfaces that inhibits the access of oxygen to the hot metal surfaces of the substrates
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The physicochemical reason for ThT fluorescence in the presence of amyloid fibrils is not known (LeVine, 1993)
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The features can be classified as: parallel tubular fibers, twisted ribbonlike structures, rod bundles, and ropelike textures
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In the 70°C samples, semicircles and sinusoidal bends are observed
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) Miner ME, Cabrera JA, Ford E, et al
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Moreover, it indicates the importance of stating explicitly the methodologies and evidence on which dietary analyses of raptors are based
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