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Titlebook: Alcohol and Aldehyde Metabolizing Systems-IV; Ronald G. Thurman Book 1980 The Editor(s) (if applicable) and The Author(s), under exclusive

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https://doi.org/10.1007/978-1-4842-5574-2ll-trans retinaldehyde by the enzyme horse liver alcohol dehydrogenase. We observe a K.. value of 145μ. and a turnover number of 0.45s. for the oxidation of all-trans retinol in the presence of Triton X-100, a surfactant used as a solubilizer. Over the concentration range of surfactant used (up to 0
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https://doi.org/10.1007/978-3-319-10247-4e with all isozymes. The reversible dehydrogenation of alcohols takes place via a random mechanism with a pathway for the formation of enzyme-NADH-alcohol complex which is simplified to an ordered BiBi mechanism at low alcohol concentrations. The same mechanism was followed by the irreversible dismu
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Lei Xu,Chunxiao Jiang,Yi Qian,Yong Reners (Fe, Cu, Cd), totally inhibited by Hg, and not significantly affected by still others (Zn, Ni, Co). Steady-state kinetics show that with 0.5 mM Mg or Mn a 2-fold activation of the velocity measured at pH 7.5 occurs when propionaldehyde is the substrate. In the pre-steady state, the magnitude bur
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Data Organization in Parallel Computers P-450 isozymes differ in their minimum molecular weights, spectral, catalytic, immunological and structural properties. NADPH-cytochrome . reductase, a flavoprotein, has also been purified and characterized (Vermilion and Coon, 1978; Gum and Strobel, 1979; Yasukochi et al., 1979).
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James Reinders,Ben Ashbaugh,Xinmin Tianrats pretreated with the reagents eliminated ethanol in blood more slowly than those not treated, and the specific activity of alcohol dehydrogenase in liver homogenates of treated animals was decreased. It appears that the design of active-site-directed reagents is feasible, but these reagents must be improved so that they are more efficacious ..
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