Xenobiotica; the fate of foreign compounds in biological systems, 38(9), 1177-1190 (2008-07-09)
1. This study investigates the enzymatic reduction of N-hydroxylated amidines by porcine adipose tissue and the possible involvement of stearoyl-CoA desaturase (SCD). 2. The reduction of the model substrate benzamidoxime was studied with porcine adipose tissue microsomes and partially purified
Archiv der Pharmazie, 322(7), 431-435 (1989-07-01)
At pH 7.4 neither benzamidine (1) is ring-hydroxylated nor benzamidoxime (2) is N-hydroxylated, reduced or ring-hydroxylated by aerobic incubations with microsomal fractions (12000 g supernatant, microsomes) of rabbit liver homogenates and NADPH. Products of hydrolytic processes are also not detected.
1,2,4-Oxadiazoles have been prepared in parallel using 1,1'-carbonyldiimidazole (CDI) as a reagent for both formation and cyclodehydration of O-acyl benzamidoximes. The use of CDI facilitates parallel purification of the oxadiazole products by simple liquid-liquid extraction and filtration.
Journal of cancer research and clinical oncology, 114(4), 363-368 (1988-01-01)
The genotoxic potentials of benzamidine and benzamidoxime were determined to study the toxicological relevance of the metabolic N-oxygenation (N-hydroxylation) of benzamidines to benzamidoximes. Benzamidoxime induced DNA single-strand breaks (in rat hepatocytes) and DNA amplification in SV40-transformed hamster cells. In the
The Journal of biological chemistry, 272(31), 19615-19620 (1997-08-01)
Drugs containing strong basic nitrogen functional groups can be N-oxygenated to genotoxic products. While the reduction of such products is of considerable toxicological significance, most in vitro studies have focused on oxygen-sensitive reductase systems. However, an oxygen-insensitive microsomal hydroxylamine reductase
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