[State of microsomal oxidation enzymes as a function of acetyltransferase activity].
Quantity and activity of components in the monoxygenase system of the liver microsomes have been studied for their dependence on the phenotype of acetylation. Results of investigations are presented. The majority of these enzymes exist as numerous molecular forms: isozymes. It is shown that activity of aminopyrine-N-demethylase and NADPH-cytochrome P-450 reductase depends on the phenotype of acetyltransferase.
Rudaia
N V
NV
Syvachenko
O E
OE
Alferov
A N
AN
Bychkar'
E M
EM
Korzhov
V I
VI
D000123:Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D000633:Aminopyrine N-Demethylase / Q000378:metabolism; D000815:Aniline Hydroxylase / Q000378:metabolism; D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D005260:Female; D014644:Genetic Variation; D006168:Guinea Pigs; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D010084:Oxidation-Reduction; D010641:Phenotype; D013250:Steroid Hydroxylases / Q000378:metabolism*
D007527:Isoenzymes; D003577:Cytochrome P-450 Enzyme System; D013250:Steroid Hydroxylases; D000815:Aniline Hydroxylase; D000633:Aminopyrine N-Demethylase; D000123:Acetyltransferases
Sostoianie sistemy fermentov mikrosomal'nogo okisleniia v zavisimosti ot atsetiltransferaznoĭ aktivnosti.