[Interaction of 2,6-dimethyl-3,5-dicarbethoxy-1,4-dihydropyridine with enzymes of the NADP.H2-specific electron transport chain of rat liver microsomes]. / Vzaimodeistvie 2,6-dimetil-3,5-dikarbetoksi-1,4-digidropiridina s fermentami NADF.H2-spetsifichnoi tsepi perenosa élektronov mikrosom pecheni krys.

2,6-Dimethyl-3,5-dicarboethoxy-1,4-dihydropyridine (DHP) interacts with NADPH-dependent electron transfer system of rat liver microsomes: it forms a complex with the terminal oxidase-cytochrome P-450, according to type I, and inhibits clearly the activity of NADPH-cytochromes c-reductase and mitindione dimethylesterase. DHP repeatedly administered in vivo rendered no inducing influence upon the microsomal enzymes.

[Participation of non-specific rat liver microsome oxidases in destruction of Nl-furanidylpyrimidines]. / Uchastie nespetsificheskikh oksidaz mikrosom pecheni krys v razrushenii Nl-furanidilpirimidinov

N1-(3'-Butyrolactono)-5-fluorouracil, N1-(2'-furanidyl) 5-trifluoromethyluracil, N1-(2'-furanidyl)-5-fluoracil are split in the rat organism with the formation of free 5-fluorouracil. The destruction of the C--N bonds in the molecule of the N1-(2'-furanidyl)-5-fluoracil takes place in the liver microsomes. This process is strengthened by NADPH and weakened by SKF-525A. All the three furanidylpyrimidines studied induced differential spectra of type I in the suspension of the liver microsomes. This fact testifies to the interaction of these substances with the cytochrome P-450.