rhodanine and Monieziasis

rhodanine has been researched along with Monieziasis* in 1 studies

Other Studies

1 other study(ies) available for rhodanine and Monieziasis

Article	Year
The metabolism of nitrophenolic and 5-arylazorhodanine anthelmintics by Ascaris suum, Moniezia expansa and by mouse- and sheep-liver enzymes. Xenobiotica; the fate of foreign compounds in biological systems, 1979, Volume: 9, Issue:8 1. The anthelmintics disophenol (2,6-diiodo-4-nitrophenol), nitroxynil (3-iodo-4-hydroxy-5-nitrobenzonitrile) and nitrodan (3-methyl-5-(4-nitrophenylazo)rhodanine) were reduced in vitro to the corresponding amines by intact Ascaris suum, Moniezia expansa, by enzymes prepared from these helminths, and by mouse- and sheep-liver homogenates. Helminth reductases required NADH2 and glutathione as cofactors and were inhibited about 50% by 2.0 x 10(-7) M allopurinol. Azo bonds of nitrodan and its analogues were not reduced by the helminths but were reduced by mouse- and sheep-liver enzymes. 2. Mouse- and sheep-liver enzymes, in addition to effecting nitro reduction, metabolized nitroxynil by hydrolysis to 3-iodo-4-hydroxy-5-nitrobenzamide and 3-iodo-4-hydroxy-5-nitrobenzoic acid. No hydroxylation products were found. Nitrodan was oxidized by the mammalian microsomal oxidation enzyme system to the thiazolidinedione derivative, but not by helminth enzymes. Topics: Animals; Anthelmintics; Ascaris; Cestoda; In Vitro Techniques; Liver; Male; Mice; Monieziasis; Nitrophenols; Nitroxinil; Rhodanine; Sheep; Species Specificity; Thiazoles	1979

Article

Year

The metabolism of nitrophenolic and 5-arylazorhodanine anthelmintics by Ascaris suum, Moniezia expansa and by mouse- and sheep-liver enzymes.

Xenobiotica; the fate of foreign compounds in biological systems, 1979, Volume: 9, Issue:8

1. The anthelmintics disophenol (2,6-diiodo-4-nitrophenol), nitroxynil (3-iodo-4-hydroxy-5-nitrobenzonitrile) and nitrodan (3-methyl-5-(4-nitrophenylazo)rhodanine) were reduced in vitro to the corresponding amines by intact Ascaris suum, Moniezia expansa, by enzymes prepared from these helminths, and by mouse- and sheep-liver homogenates. Helminth reductases required NADH2 and glutathione as cofactors and were inhibited about 50% by 2.0 x 10(-7) M allopurinol. Azo bonds of nitrodan and its analogues were not reduced by the helminths but were reduced by mouse- and sheep-liver enzymes. 2. Mouse- and sheep-liver enzymes, in addition to effecting nitro reduction, metabolized nitroxynil by hydrolysis to 3-iodo-4-hydroxy-5-nitrobenzamide and 3-iodo-4-hydroxy-5-nitrobenzoic acid. No hydroxylation products were found. Nitrodan was oxidized by the mammalian microsomal oxidation enzyme system to the thiazolidinedione derivative, but not by helminth enzymes.

Topics: Animals; Anthelmintics; Ascaris; Cestoda; In Vitro Techniques; Liver; Male; Mice; Monieziasis; Nitrophenols; Nitroxinil; Rhodanine; Sheep; Species Specificity; Thiazoles

1979