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1 published report, is efficiently reduced by NADPH-P450 reductase.
2 a cells with the genes encoding P450 2B6 and NADPH-P450 reductase.
3 a reconstituted system with purified rabbit NADPH-P450 reductase.
4 osomal activation of 3-NBA was attributed to NADPH: p450 reductase.
5 nicotinamide adenine dinucleotide phosphate (NADPH)-P450 reductases.
6 te for the first time the potential of human NADPH: p450 reductase and recombinant p450s to contribut
7 , a fusion protein in which it was linked to NADPH-P450 reductase, and baculovirus and bacterial memb
8 caused in part to lower binding affinity for NADPH-P450 reductase, but the K476E mutant did not achie
9 perties, along with a protocol for measuring NADPH-P450 reductase by its NADPH-cytochrome c reduction
11 The transient intermediate observed in the NADPH-P450 reductase-catalyzed reaction accumulated when
12 atterns of activity plotted as a function of NADPH-P450 reductase concentration in systems containing
13 ovel triple transgenic mouse model, with the NADPH-P450 reductase (Cpr) gene deleted in a lung-specif
14 using a reconstitution system consisting of NADPH-P450 reductase (CPR), dioleoylphosphatidylcholine
15 We conclude that the P450 systems utilizing NADPH-P450 reductase, cumene hydroperoxide, and iodosylb
16 E. coli membranes containing each P450 (with NADPH-P450 reductase expressed using a bicistronic vecto
17 purified rabbit enzyme and recombinant human NADPH: p450 reductase expressed in Chinese hamster V79 c
19 1B1, 2A6, 2B6, 2D6, 2C9, 2E1, and 3A4 and of NADPH: p450 reductase in the metabolic activation of 3-N
20 role of specific cytochromes p450 (p450) and NADPH:p450 reductase in the human hepatic microsomal sam
21 as investigated by correlating the p450- and NADPH: p450 reductase-linked catalytic activities in eac
22 either iodosylbenzene (PhIO) or a mixture of NADPH-P450 reductase, NADPH, and O2, (iii) horseradish p
23 dation products formed in systems containing NADPH-P450 reductase/NADPH and the model oxidant cumene
24 re P450 reactions involving the normal NADPH/NADPH-P450 reductase/O2 system with those supported by t
26 , and V322A proteins were reconstituted with NADPH-P450 reductase, rates of 7-ethoxyresorufin O-deeth
27 ndent on electron input from the flavoenzyme NADPH-P450 reductase (RED), which is widely expressed in
30 0 nmol per liter culture, with expression of NADPH-P450 reductase typically ranging from 50% to 100%
31 re modified considerably in systems in which NADPH-P450 reductase was replaced with a flavodoxin or f
32 nd bacterial membranes in which P450 3A4 and NADPH-P450 reductase were coexpressed; the systems diffe
33 main of P450 BM3) or a truncated form of rat NADPH-P450 reductases were expressed in Escherichia coli
34 rate-O(2) complex was slow in the absence of NADPH-P450 reductase, with a first-order rate constant o
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