Journal of pharmacobio-dynamics, 4(2), 101-108 (1981-02-01)
The electron transfer mechanism in the reduction of aromatic nitro compounds by xanthine oxidase was investigated using methyl p-nitrobenzoate and p-nitroacetophenone as substrates. Methyl p-nitrobenzene was reduced by both one-electron and more than two-electron transfer mechanisms in the enzyme-electron donor
[Semiconservative and unscheduled DNA-synthesis of rat thymocytes under the influence of some radioprotecting and radiosensitizing agents (author's transl)].
The enzyme family carbonyl reductase, which catalyses the reduction of xenobiotic as well as endogenous ketones and aldehydes, has not been very well studied in terms of its biological functions and structural aspects. The aim of the present study was
International journal of radiation biology and related studies in physics, chemistry, and medicine, 39(1), 63-71 (1981-01-01)
The reactions of the one electron adduct of 2'-deoxyadenosine dA(-), in aqueous solutions have been studied using pulse radiolysis techniques with optical absorption and conductivity detection. The dA(-) radical anion itself shows a weak and featureless optical absorption at greater
Interindividual variability of carbonyl reductase levels in human livers (N = 11) was examined by measuring reductase activity toward various substrates and by western blot analysis using anti-rat ovarian carbonyl reductase CR2 antibody. The carbonyl reductase activity toward p-nitrobenzaldehyde (PNBA)
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