Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
Article in English | MEDLINE | ID: mdl-6806354

ABSTRACT

The authors studied combined effect of aniline (20 mg/kg for a period of 4 weeks in drinking water) and nitrosodimethylamine (NDMA) (30 mg/kg, a single intragastric dose) on the activity of enzymes of different subcellular structures: endoplasmic reticulum (cytochromes P450, B5, acetylesterase), mitochondria (malate dehydrogenase) and the content of N-acetylneuraminic acid in rat liver and of lysosomes (beta-glucuronidase, beta-galactosidase). The combined action of NDMA and aniline was accompanied by more pronounced changes in the indices under investigation than isolated administration of the given chemical substances. The most pronounced aggravation of the unfavourable changes was observed in the activity of enzymes connected with the processes of oxidation and energy supply to the cell (malate dehydrogenase) and the metabolism of glucuronides (beta-glucuronidase) as well as in the content of N-acetylneuraminic acid. This may be connected with the modifying effect of aniline on the toxic effect of NDMA.


Subject(s)
Aniline Compounds/pharmacology , Dimethylnitrosamine/pharmacology , Lysosomes/enzymology , Microsomes, Liver/enzymology , Acetylesterase/metabolism , Animals , Cytochrome P-450 Enzyme System/metabolism , Glucuronidase/metabolism , Liver/enzymology , Liver/metabolism , Liver/ultrastructure , Malate Dehydrogenase/metabolism , Male , Rats , Sialic Acids/metabolism , beta-Galactosidase/metabolism
2.
Article in English | MEDLINE | ID: mdl-7190985

ABSTRACT

The authors performed a comparative biochemical study of some enzymes of lysosomic origin (hyaluronidase, N-acetyl-beta-D-glucosaminidase, beta-glucosidase, beta-galatosidase and acid phosphatase), of the state of enzyme substrate system N-acetylneuraminic acid---aldolase of neuramic acid and of the activity of lactatedehydrogenase (soluble in cytosol and bound on mitochodria) in the liver, lungs and blood serum of rats at various regimens of the inhalation action of CCl4. On the basis of results obtained they determined the biological importance of the change of activity of enzymes differently localized in cells at the adaptation of an organisme to the noxious action of CCl4.


Subject(s)
Carbon Tetrachloride/pharmacology , Fructose-Bisphosphate Aldolase/metabolism , Hydrolases/metabolism , L-Lactate Dehydrogenase/metabolism , Liver/enzymology , Animals , Cytoplasm/enzymology , Liver/ultrastructure , Lung/enzymology , Lysosomes/enzymology , Male , Rats
SELECTION OF CITATIONS
SEARCH DETAIL
...