PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9321518-5 1997 The involvement of cytochrome b5 in the formation of N-acetyl-p-benzoquinone imine (NAPQI) was implicated through a synergistic effect of NADH on the NADPH-supported reaction. NAD 138-142 cytochrome b5 type A Rattus norvegicus 19-32 8600980-14 1996 These results indicate that P-450, and to a lesser extent, cytochrome b5, play a role in the ferritin-dependent increase in formation of reactive oxygen species with either NADPH or NADH, most likely reflecting the requirement of these enzymes for microsomal production of superoxide anion. NAD 182-186 cytochrome b5 type A Rattus norvegicus 59-72 8812833-6 1996 The recombinant domain retained both NADH:ferricyanide and NADH:cytochrome b5 reductase activities with Vmax of 48 and 26 micromol NADH consumed/min/nmol FAD, respectively, and Km of 6, 7, and 11 microM for NADH, ferricyanide, and cytochrome b5. NAD 37-41 cytochrome b5 type A Rattus norvegicus 64-77 8812833-6 1996 The recombinant domain retained both NADH:ferricyanide and NADH:cytochrome b5 reductase activities with Vmax of 48 and 26 micromol NADH consumed/min/nmol FAD, respectively, and Km of 6, 7, and 11 microM for NADH, ferricyanide, and cytochrome b5. NAD 37-41 cytochrome b5 type A Rattus norvegicus 231-244 8812833-6 1996 The recombinant domain retained both NADH:ferricyanide and NADH:cytochrome b5 reductase activities with Vmax of 48 and 26 micromol NADH consumed/min/nmol FAD, respectively, and Km of 6, 7, and 11 microM for NADH, ferricyanide, and cytochrome b5. NAD 59-63 cytochrome b5 type A Rattus norvegicus 64-77 8812833-6 1996 The recombinant domain retained both NADH:ferricyanide and NADH:cytochrome b5 reductase activities with Vmax of 48 and 26 micromol NADH consumed/min/nmol FAD, respectively, and Km of 6, 7, and 11 microM for NADH, ferricyanide, and cytochrome b5. NAD 59-63 cytochrome b5 type A Rattus norvegicus 231-244 8812833-6 1996 The recombinant domain retained both NADH:ferricyanide and NADH:cytochrome b5 reductase activities with Vmax of 48 and 26 micromol NADH consumed/min/nmol FAD, respectively, and Km of 6, 7, and 11 microM for NADH, ferricyanide, and cytochrome b5. NAD 59-63 cytochrome b5 type A Rattus norvegicus 64-77 8812833-6 1996 The recombinant domain retained both NADH:ferricyanide and NADH:cytochrome b5 reductase activities with Vmax of 48 and 26 micromol NADH consumed/min/nmol FAD, respectively, and Km of 6, 7, and 11 microM for NADH, ferricyanide, and cytochrome b5. NAD 59-63 cytochrome b5 type A Rattus norvegicus 231-244 8812833-6 1996 The recombinant domain retained both NADH:ferricyanide and NADH:cytochrome b5 reductase activities with Vmax of 48 and 26 micromol NADH consumed/min/nmol FAD, respectively, and Km of 6, 7, and 11 microM for NADH, ferricyanide, and cytochrome b5. NAD 59-63 cytochrome b5 type A Rattus norvegicus 64-77 8812833-6 1996 The recombinant domain retained both NADH:ferricyanide and NADH:cytochrome b5 reductase activities with Vmax of 48 and 26 micromol NADH consumed/min/nmol FAD, respectively, and Km of 6, 7, and 11 microM for NADH, ferricyanide, and cytochrome b5. NAD 59-63 cytochrome b5 type A Rattus norvegicus 231-244 1552368-3 1992 By mixing the purified cytochrome b5 with cytochrome b5 reductase, cob(II)alamin was immediately formed from aquacobalamin and NADH. NAD 127-131 cytochrome b5 type A Rattus norvegicus 23-36 8175767-1 1994 A gene has been constructed coding for a chimeric flavocytochrome b5 protein that comprises the soluble domain of rat hepatic cytochrome b5 as the NH2-terminal portion of the chimera and the flavin-containing domain of spinach assimilatory NADH:nitrate reductase as the C terminus. NAD 240-244 cytochrome b5 type A Rattus norvegicus 55-68 1552368-2 1992 Microsomal NADH-linked aquacobalamin reductase, which was solubilized with 10 g/L sodium deoxycholate, showed identical elution behavior to NADH-cytochrome c reductase (cytochrome b5/cytochrome b5 reductase complex) on DEAE-Toyopearl 650 column chromatography. NAD 11-15 cytochrome b5 type A Rattus norvegicus 169-182 1552368-2 1992 Microsomal NADH-linked aquacobalamin reductase, which was solubilized with 10 g/L sodium deoxycholate, showed identical elution behavior to NADH-cytochrome c reductase (cytochrome b5/cytochrome b5 reductase complex) on DEAE-Toyopearl 650 column chromatography. NAD 11-15 cytochrome b5 type A Rattus norvegicus 183-196 1552368-3 1992 By mixing the purified cytochrome b5 with cytochrome b5 reductase, cob(II)alamin was immediately formed from aquacobalamin and NADH. NAD 127-131 cytochrome b5 type A Rattus norvegicus 42-55 1552368-4 1992 These results provide evidence that the NADH-linked aquacobalamin reductase activity is derived from the cytochrome b5/cytochrome b5 reductase complex in rat liver microsomes. NAD 40-44 cytochrome b5 type A Rattus norvegicus 105-118 1552368-4 1992 These results provide evidence that the NADH-linked aquacobalamin reductase activity is derived from the cytochrome b5/cytochrome b5 reductase complex in rat liver microsomes. NAD 40-44 cytochrome b5 type A Rattus norvegicus 119-132 1710590-1 1990 Calf thymus DNA was incubated with bleomycin and FeCl3 in the presence of isolated rat liver microsomal NADH-cytochrome b5 reductase, cytochrome b5 and NADH which catalyze redox cycling of the bleomycin-Fe-complex. NAD 104-108 cytochrome b5 type A Rattus norvegicus 109-122 2345545-2 1990 The NADH reduced cytochrome b5 (cyt b5)4 spectrum of these cells was similar to rat liver cyt b5. NAD 4-8 cytochrome b5 type A Rattus norvegicus 17-30 2345545-2 1990 The NADH reduced cytochrome b5 (cyt b5)4 spectrum of these cells was similar to rat liver cyt b5. NAD 4-8 cytochrome b5 type A Rattus norvegicus 32-38 2540809-10 1989 Both of the reconstituted proteins were found to be capable of transferring electrons to cytochrome c in a reconstituted system dependent on NADH and cytochrome b5 reductase, thus stimulating the activity of native cytochrome b5. NAD 141-145 cytochrome b5 type A Rattus norvegicus 215-228 3116769-1 1987 After administration into rats of folic acid at a dose of 25 mg/kg within 14 days activities of NADPH-cytochrome P-450 and NADH-cytochrome b5 reductases, content of cytochromes P-450 and b5 as well as the rates of NADPH and NADH oxidation were increased in liver microsomes. NAD 123-127 cytochrome b5 type A Rattus norvegicus 128-141 3935115-1 1985 This study compared the NADH- and NADPH-supported p-nitrophenetole (NP) O-deethylase, ethylmorphine (EM) O-deethylase and EM N-demethylase activities of rat hepatic microsomes with respect to dioxygen requirement, inhibition by carbon monoxide, inhibition by classical inhibitors of cytochrome P-450 systems, and the involvement of NADH-cytochrome b5, cytochrome b5 reductase and NADPH-cytochrome P-450 reductase. NAD 24-28 cytochrome b5 type A Rattus norvegicus 337-350 3803575-3 1986 NADH-supported reduction of cytochrome b5 was also inhibited by propylthiouracil in the reconstituted system consisting of cytochrome b5 and partially purified NADH-cytochrome b5 reductase. NAD 0-4 cytochrome b5 type A Rattus norvegicus 28-41 3803575-3 1986 NADH-supported reduction of cytochrome b5 was also inhibited by propylthiouracil in the reconstituted system consisting of cytochrome b5 and partially purified NADH-cytochrome b5 reductase. NAD 0-4 cytochrome b5 type A Rattus norvegicus 123-136 3803575-3 1986 NADH-supported reduction of cytochrome b5 was also inhibited by propylthiouracil in the reconstituted system consisting of cytochrome b5 and partially purified NADH-cytochrome b5 reductase. NAD 0-4 cytochrome b5 type A Rattus norvegicus 123-136 3935115-1 1985 This study compared the NADH- and NADPH-supported p-nitrophenetole (NP) O-deethylase, ethylmorphine (EM) O-deethylase and EM N-demethylase activities of rat hepatic microsomes with respect to dioxygen requirement, inhibition by carbon monoxide, inhibition by classical inhibitors of cytochrome P-450 systems, and the involvement of NADH-cytochrome b5, cytochrome b5 reductase and NADPH-cytochrome P-450 reductase. NAD 24-28 cytochrome b5 type A Rattus norvegicus 352-365 3935115-5 1985 The use of antibodies against NADPH-cytochrome P-450 reductase, NADH-cytochrome b5 reductase and cytochrome b5 demonstrated that both the NADH- and the NADPH-supported reactions depend on established components of cytochrome P-450 systems. NAD 64-68 cytochrome b5 type A Rattus norvegicus 69-82 2995584-2 1985 Mercuric chloride and p-chloromercuriphenylsulfonate, inhibitors on NADH-cytochrome b5 reductase, at 32 microM inhibited NADH-supported palmitoyl-CoA elongation to 30 and 60% of control activity, respectively, whereas NADPH-supported palmitoyl-CoA elongation was unaffected by these mercurials. NAD 68-72 cytochrome b5 type A Rattus norvegicus 73-86 2995584-3 1985 An antibody to rat liver NADH-cytochrome b5 reductase inhibited brain microsomal NADH-cytochrome b5 reductase activity and NADH-dependent palmitoyl-CoA elongation. NAD 25-29 cytochrome b5 type A Rattus norvegicus 30-43 2995584-3 1985 An antibody to rat liver NADH-cytochrome b5 reductase inhibited brain microsomal NADH-cytochrome b5 reductase activity and NADH-dependent palmitoyl-CoA elongation. NAD 25-29 cytochrome b5 type A Rattus norvegicus 86-99 2995584-6 1985 These results indicate the presence of an electron transport system, NADH-NADH-cytochrome b5 reductase-cytochrome b5-fatty acid elongation, in brain microsomes. NAD 69-73 cytochrome b5 type A Rattus norvegicus 79-92 2995584-6 1985 These results indicate the presence of an electron transport system, NADH-NADH-cytochrome b5 reductase-cytochrome b5-fatty acid elongation, in brain microsomes. NAD 69-73 cytochrome b5 type A Rattus norvegicus 103-116 6489918-4 1984 Furthermore, the rate of the NADH-depending lathosterol 5-desaturation in the reconstitution system, was proportional to the concentration either of the terminal desaturase, cytochrome b5, or NADH-cytochrome b5 reductase, under conditions in which other enzymes were present in excess. NAD 29-33 cytochrome b5 type A Rattus norvegicus 174-187 6489918-4 1984 Furthermore, the rate of the NADH-depending lathosterol 5-desaturation in the reconstitution system, was proportional to the concentration either of the terminal desaturase, cytochrome b5, or NADH-cytochrome b5 reductase, under conditions in which other enzymes were present in excess. NAD 29-33 cytochrome b5 type A Rattus norvegicus 197-210 6376489-3 1984 This microsomal reductase converts acetoacetyl-CoA to beta-hydroxybutyryl-CoA at a rate of 70 nmol/min/mg of protein; the enzyme has a specific requirement for NADH and appears to obtain electrons directly from the reduced pyridine nucleotide without the intervention of cytochrome b5 and its flavoprotein reductase. NAD 160-164 cytochrome b5 type A Rattus norvegicus 271-284 6537216-10 1984 Both ethanol and phenobarbital elevated cytochrome P-450; ethanol also elevated cytochrome b5 measured as NADH-reducible cytochrome. NAD 106-110 cytochrome b5 type A Rattus norvegicus 80-93 6425273-4 1984 Addition of NADH to the NADPH-supported oxygenase assay system enhanced both steroid oxygenase activities, and addition of the antibody against cytochrome b5 decreased the NADH-caused stimulation of steroid 17 alpha-hydroxylase and C-17-C-20 lyase activities. NAD 172-176 cytochrome b5 type A Rattus norvegicus 144-157 6425273-5 1984 When dehydroepiandrosterone and NAD+ were added as substrates for 3 beta-hydroxy-delta 5-steroid dehydrogenase in order to synthesize NADH by enzymatic reaction, the NADPH-supported activities of steroid 17 alpha-hydroxylase and C-17-C-20 lyase were further stimulated as compared with the addition of NADH, and this stimulation was suppressed by the antibody against cytochrome b5. NAD 32-36 cytochrome b5 type A Rattus norvegicus 368-381 6425273-5 1984 When dehydroepiandrosterone and NAD+ were added as substrates for 3 beta-hydroxy-delta 5-steroid dehydrogenase in order to synthesize NADH by enzymatic reaction, the NADPH-supported activities of steroid 17 alpha-hydroxylase and C-17-C-20 lyase were further stimulated as compared with the addition of NADH, and this stimulation was suppressed by the antibody against cytochrome b5. NAD 134-138 cytochrome b5 type A Rattus norvegicus 368-381 6654894-3 1983 The rate of reoxidation of NADH-reduced microsomal cytochrome b5 was markedly stimulated (up to 3-fold) by the addition of increasing concentrations of beta-ketohexadecanoyl-CoA (1-8 microM). NAD 27-31 cytochrome b5 type A Rattus norvegicus 51-64 6654894-8 1983 Although trans-2-hexadecenoyl-CoA significantly stimulated the NADH-reduced cytochrome b5 reoxidation rate under aerobic conditions, it did not have any stimulatory effect under anaerobic conditions. NAD 63-67 cytochrome b5 type A Rattus norvegicus 76-89 6444203-6 1983 Thus the reduction of cytochrome b5 by NADH and NADPH is the diffusion-dependent reaction in the redox-chains of microsomes only. NAD 39-43 cytochrome b5 type A Rattus norvegicus 22-35 6119752-7 1981 It is concluded that bromotrichloromethane and 1,2-dibromo-1,2-dichloroethane stimulate hepatic microsomal electron transfer from NADH via cytochrome b-5 by interacting with cytochrome P-450 and with stearate desaturase. NAD 130-134 cytochrome b5 type A Rattus norvegicus 139-153 6305359-3 1983 NADH-synergistic effect decreased in parallel with the decrease of the ratio of cytochrome b5/cytochrome P-450 in liver microsomes. NAD 0-4 cytochrome b5 type A Rattus norvegicus 80-93 6830827-4 1983 Also, we find that a fragment of rat liver NADH-cytochrome b5 reductase can restore NADH-dependent cytochrome b5 reduction to Tetrahymena microsomes which have been treated with N-ethylmaleimide to eliminate endogenous reductase activity. NAD 43-47 cytochrome b5 type A Rattus norvegicus 48-61 6830827-4 1983 Also, we find that a fragment of rat liver NADH-cytochrome b5 reductase can restore NADH-dependent cytochrome b5 reduction to Tetrahymena microsomes which have been treated with N-ethylmaleimide to eliminate endogenous reductase activity. NAD 43-47 cytochrome b5 type A Rattus norvegicus 99-112 6806275-6 1982 Thus, microsomal cytochrome P-450 appears to be reduced via two independent pathways of electron transport from NADH; the biphasic reduction occurs via cytochrome P-450 reductase while the slower monophasic reduction occurs via cytochrome b5. NAD 112-116 cytochrome b5 type A Rattus norvegicus 228-241 7260196-5 1981 Hence only the reactions of cytochrome b5 reduction by NADH- and NADPH-specific flavoproteins are diffusion-dependent processes in the microsomal oxidation chain. NAD 55-59 cytochrome b5 type A Rattus norvegicus 28-41 7228857-10 1981 These results strongly support the suggestion that membrane-bound cytochrome b5 of rat liver microsomes is an obligatory electron carrier from NADH to 4-methyl sterol oxidase. NAD 143-147 cytochrome b5 type A Rattus norvegicus 66-79 7391131-0 1980 Localization and biosynthesis of NADH-cytochrome b5 reductase, an integral membrane protein, in rat liver cells. NAD 33-37 cytochrome b5 type A Rattus norvegicus 38-51 6778467-5 1980 The V values at different NADH concentrations appeared to correlate with the concentration of reduced cytochrome b5 that the added NADH could sustain during the incubation period. NAD 26-30 cytochrome b5 type A Rattus norvegicus 102-115 43909-1 1979 These studies have shown that addition of p-nitroanisole to a reaction mixture containing rat liver microsomes resulted in an increase the reoxidation rate of NADH-reduced cytochrome b5. NAD 159-163 cytochrome b5 type A Rattus norvegicus 172-185 43909-2 1979 Fortification of rat liver microsomes with partially purified cytochrome b5 produces an increase in both NADPH-dependent and NADH-dependent p-nitroanisole O-demethylation activity. NAD 125-129 cytochrome b5 type A Rattus norvegicus 62-75 43909-5 1979 These results suggest that NADH-dependent and, in part, NADPH-dependent O-demethylations are catalyzed by cytochrome P-448 and cytochrome P-450 receiving electrons from cytochrome b5. NAD 27-31 cytochrome b5 type A Rattus norvegicus 169-182 6778467-5 1980 The V values at different NADH concentrations appeared to correlate with the concentration of reduced cytochrome b5 that the added NADH could sustain during the incubation period. NAD 131-135 cytochrome b5 type A Rattus norvegicus 102-115 6778467-6 1980 Tetrahydronicotinamide adenine dinucleotide (NADH3), a structural analogue of NADH, reduced demethylase activity without affecting NADPH-cytochrome P450 reductase activity or the concentration of reduced cytochrome b5. NAD 45-49 cytochrome b5 type A Rattus norvegicus 204-217 24622-3 1978 Antibodies to NADH-cytochrome b5 reductase [EC 1.6.2.2] and cytochrome b5 inhibited NADH-dependent lipid peroxidation in the presence of ADP-Fe, whereas the antibody against NADPH-cytochrome c reductase [EC 1.6.2.4] showed no inhibition. NAD 14-18 cytochrome b5 type A Rattus norvegicus 19-32 24622-4 1978 These oberservations suggest that the electron from NADH was supplied to the lipid peroxidation reaction via NADH-cytochrome b5 reductase and cytochrome b5. NAD 52-56 cytochrome b5 type A Rattus norvegicus 114-127 24622-4 1978 These oberservations suggest that the electron from NADH was supplied to the lipid peroxidation reaction via NADH-cytochrome b5 reductase and cytochrome b5. NAD 52-56 cytochrome b5 type A Rattus norvegicus 142-155 8453-2 1976 The three purified proteins which are required for microsomal stearyl-CoA desaturation, NADH-cytochrome b5 reductase, cytochrome b5, and desaturase, have been combined with egg lecithin or dimyristyl lecithin vesicles to reconstruct a functional electron transport system capable of utilizing NADH and O2 in the desaturation of stearyl-CoA. NAD 88-92 cytochrome b5 type A Rattus norvegicus 93-106 27110038-3 2016 We also studied the effectiveness of coenzymes of two of the microsomal reductases, NADPH as a coenzyme of POR, and NADH as a coenzyme of NADH:cytochrome b5 reductase, to mediate BaP metabolism in these systems. NAD 116-120 cytochrome b5 type A Rattus norvegicus 143-156 2319-1 1976 In a number of animal species soluble NADH-cytochrome b5 reductase of erythrocytes was compared with membrane-bound NADH-cytochrome b5 reductase of liver microsomes by using an antibody to purified NADH-cytochrome b5 reductase from rat liver microsomes. NAD 38-42 cytochrome b5 type A Rattus norvegicus 43-56 1191670-2 1975 Incubation of rat homogeneous detergent-solubilized cytochrome b5 with rat liver microsomes resulted in specific binding of the hemoprotein which was rapidly reduced by NADH. NAD 169-173 cytochrome b5 type A Rattus norvegicus 52-65 1191670-4 1975 However, the extra-bound detergent-solubilized cytochrome b5 did inhibit NADPH-dependent N-demethylations, the NADH synergism and NADPH cytochrome P-450 reductase activity. NAD 111-115 cytochrome b5 type A Rattus norvegicus 47-60 175045-10 1975 In contrast to the reoxidation of beta-NADH-reduced cytochrome b5, the process was largely monophasic when cytochrome b5 was reduced with alpha-NADH. NAD 34-43 cytochrome b5 type A Rattus norvegicus 52-65 175045-10 1975 In contrast to the reoxidation of beta-NADH-reduced cytochrome b5, the process was largely monophasic when cytochrome b5 was reduced with alpha-NADH. NAD 34-43 cytochrome b5 type A Rattus norvegicus 107-120 1175656-7 1975 On the other hand, the oxidation of cytochrome b5 by hydroperoxides is readily demonstrable in microsomal fractions in presence of NADH. NAD 131-135 cytochrome b5 type A Rattus norvegicus 36-49 27110038-7 2016 In the presence of either of the reductase cofactors tested, NADPH or NADH, cytochrome b5 stimulated CYP1A1-mediated formation of both BaP-DNA adducts. NAD 70-74 cytochrome b5 type A Rattus norvegicus 76-89 27110038-8 2016 The results demonstrate that NADH can act as a sole electron donor for both the first and the second reduction of CYP1A1 during its reaction cycle catalyzing oxidation of BaP, and suggest that the NADH:cytochrome b5 reductase as the NADH-dependent reductase might substitute POR in this enzymatic system. NAD 29-33 cytochrome b5 type A Rattus norvegicus 202-215 27110038-8 2016 The results demonstrate that NADH can act as a sole electron donor for both the first and the second reduction of CYP1A1 during its reaction cycle catalyzing oxidation of BaP, and suggest that the NADH:cytochrome b5 reductase as the NADH-dependent reductase might substitute POR in this enzymatic system. NAD 197-201 cytochrome b5 type A Rattus norvegicus 202-215 27110038-3 2016 We also studied the effectiveness of coenzymes of two of the microsomal reductases, NADPH as a coenzyme of POR, and NADH as a coenzyme of NADH:cytochrome b5 reductase, to mediate BaP metabolism in these systems. NAD 138-142 cytochrome b5 type A Rattus norvegicus 143-156 12821320-2 2003 All 25 currently identified type I and type II methemoglobinemia mutants have been expressed in Escherichia coli using a novel six histidine-tagged rat cytochrome b5/cytochrome b5 reductase fusion protein designated NADH:cytochrome c reductase (H6NCR). NAD 216-220 cytochrome b5 type A Rattus norvegicus 152-165 16216070-1 2005 Cytochrome b5 reductase (cb5r), a member of the ferredoxin:NADP+ reductase family of flavoprotein transhydrogenases, catalyzes the NADH-dependent reduction of cytochrome b5. NAD 131-135 cytochrome b5 type A Rattus norvegicus 0-13 16216070-1 2005 Cytochrome b5 reductase (cb5r), a member of the ferredoxin:NADP+ reductase family of flavoprotein transhydrogenases, catalyzes the NADH-dependent reduction of cytochrome b5. NAD 131-135 cytochrome b5 type A Rattus norvegicus 159-172 14503867-1 2003 Microsomal cytochrome b(5) reductase (EC 1.6.2.2) catalyzes the reduction of ferricytochrome b(5) using NADH as the physiological electron donor. NAD 104-108 cytochrome b5 type A Rattus norvegicus 11-26 14503867-5 2003 Wild-type (WT) cytochrome b(5) reductase showed a 3700-fold preference for NADH whereas the mutant with the highest NADPH efficiency, D239T, showed an 11-fold preference for NADPH, a 39200-fold increase. NAD 75-79 cytochrome b5 type A Rattus norvegicus 15-30 14503867-6 2003 Wild-type cytochrome b(5) reductase only formed a stable charge-transfer complex with NADH while D239T formed complexes with both NADH and NADPH. NAD 86-90 cytochrome b5 type A Rattus norvegicus 10-25 14503867-6 2003 Wild-type cytochrome b(5) reductase only formed a stable charge-transfer complex with NADH while D239T formed complexes with both NADH and NADPH. NAD 130-134 cytochrome b5 type A Rattus norvegicus 10-25 12821320-2 2003 All 25 currently identified type I and type II methemoglobinemia mutants have been expressed in Escherichia coli using a novel six histidine-tagged rat cytochrome b5/cytochrome b5 reductase fusion protein designated NADH:cytochrome c reductase (H6NCR). NAD 216-220 cytochrome b5 type A Rattus norvegicus 166-179