منابع مشابه
Metabolism of daunorubicin by a barbiturate-sensitive aldehyde reductase from rat liver.
A barbiturate-sensitive aldehyde reductase was purified to homogeneity from rat liver and shown to metabolize the cancer-chemotherapeutic antibiotic daunorubicin. The aldehyde reductase may have important roles in the metabolism of exogeneous drugs as well as the aldehyde derivatives of the biogenic amines.
متن کاملBiotransformations of daunorubicin aglycones by rat liver microsomes.
Daunorubicin is biotransformed anaerobically by rat liver microsomes with a reduced nicotinamide adenine dinucleotide phosphate-generating system to form a series of aglycones. The first reaction, reductive cleavage of daunosamine (at C-7 in ring A) to form the 7- deoxyaglycone , is followed by reduction of the C-13 keto group. The 7- hydroxyaglycone may also form by hydrolytic cleavage of the ...
متن کاملInitial biotransformations of daunorubicin to aglycones by rat liver microsomes.
Anaerobic incubations of rat liver microsomes convert daunorubicin into at least six or seven aglycones in the presence of reduced nicotinamide adenine dinucleotide phosphate or a reduced nicotinamide adenine dinucleotide phosphate-generating system. The partial identification of some of the aglycones is based on cochromatographs of chemically synthesized derivatives by isocratic high-pressure ...
متن کاملInitial Biotransformations of Daunorubicin to Aglycones by Rat Liver Microsomes1
Anaerobic incubations of rat liver microsomes convert daunorubicin into at least six or seven aglycones in the presence of reduced nicotinamide adenine dinucleotide phosphate or a reduced nicotinamide adenine dinucleotide phosphate-gener ating system. The partial identification of some of the aglycones is based on cochromatographs of chemically synthesized de rivatives by isocratic high-pressur...
متن کاملCrystal structure of rat liver dihydropteridine reductase.
The structure of a binary complex of dihydropteridine reductase [DHPR; NAD(P)H:6,7-dihydropteridine oxidoreductase, EC 1.6.99.7] with its cofactor, NADH, has been solved and refined to a final R factor of 15.4% by using 2.3 A diffraction data. DHPR is an alpha/beta protein with a Rossmann-type dinucleotide fold for NADH binding. Insertion of an extra threonine residue in the human enzyme is ass...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)42527-1