PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2754757-0 1989 Effect of carbon monoxide on the cytochrome P-450-mediated metabolism of aniline and p-nitroanisole in the isolated perfused rabbit lung. Carbon Monoxide 10-25 cytochrome P-450 Oryctolagus cuniculus 33-49 1912302-1 1991 The N-hydroxylation of representative aromatic amines by rabbit liver microsomes was mediated by cytochrome P-450 as demonstrated by the sensitivity to carbon monoxide and other cytochrome P-450 inhibitors. Carbon Monoxide 152-167 cytochrome P-450 Oryctolagus cuniculus 97-113 2573501-4 1989 This reaction is mediated by cytochrome P-450 as indicated by the requirement of NADPH, the incorporation of 18O, and inhibition by 10 mM metyrapone, 0.1 mM SKF 525-A, and CO/O2 (50/50, 80/20). Carbon Monoxide 172-174 cytochrome P-450 Oryctolagus cuniculus 29-45 3206526-1 1988 Carbon monoxide (CO) is a ubiquitous environmental pollutant widely recognized for its ability to inhibit cytochrome P450-mediated metabolism of xenobiotics in vitro. Carbon Monoxide 0-15 cytochrome P-450 Oryctolagus cuniculus 106-121 3206526-1 1988 Carbon monoxide (CO) is a ubiquitous environmental pollutant widely recognized for its ability to inhibit cytochrome P450-mediated metabolism of xenobiotics in vitro. Carbon Monoxide 17-19 cytochrome P-450 Oryctolagus cuniculus 106-121 3206526-3 1988 The purpose of this investigation was to establish a threshold for the CO-induced inhibition of cytochrome P450-mediated activity in the isolated perfused rabbit lung and to determine if hemoglobin would alter the carbon monoxide-cytochrome P450 interaction. Carbon Monoxide 214-229 cytochrome P-450 Oryctolagus cuniculus 230-245 2754757-1 1989 Carbon monoxide (CO), an environmental pollutant, inhibits the cytochrome P-450-mediated metabolism of xenobiotics in vitro. Carbon Monoxide 0-15 cytochrome P-450 Oryctolagus cuniculus 63-79 2754757-1 1989 Carbon monoxide (CO), an environmental pollutant, inhibits the cytochrome P-450-mediated metabolism of xenobiotics in vitro. Carbon Monoxide 17-19 cytochrome P-450 Oryctolagus cuniculus 63-79 2754757-6 1989 That these reactions are not similarly influenced by carbon monoxide may indicate that the constitutive isozymes of cytochrome P-450 in the rabbit lung are differentially sensitive to CO-induced inhibition. Carbon Monoxide 53-68 cytochrome P-450 Oryctolagus cuniculus 116-132 7319893-6 1981 These findings suggest that cytochrome P-450 could act as a carrier for O2 and CO in tissue with low PO2"s. Carbon Monoxide 79-81 cytochrome P-450 Oryctolagus cuniculus 28-44 3759928-2 1986 These activities were greatly inhibited by carbon monoxide, indicating the involvement of cytochrome P-450. Carbon Monoxide 43-58 cytochrome P-450 Oryctolagus cuniculus 90-106 6469945-6 1984 The PGA1 hydroxylase activities of the microsomes from both small intestine and colon were inhibited markedly by carbon monoxide, indicating the participation of cytochrome P-450. Carbon Monoxide 113-128 cytochrome P-450 Oryctolagus cuniculus 162-178 7142127-8 1982 This cytochrome P-450 showed a maximal peak at 448 nm in the carbon monoxide difference spectrum of its reduced form. Carbon Monoxide 61-76 cytochrome P-450 Oryctolagus cuniculus 5-21 3663229-9 1987 The direct involvement of cytochrome P-450 in this reaction is supported by the observation that the presence of inhibitors of cytochrome P-450, in particular of carbon monoxide, markedly decreased the rate of N-demethylation. Carbon Monoxide 162-177 cytochrome P-450 Oryctolagus cuniculus 26-42 3663229-9 1987 The direct involvement of cytochrome P-450 in this reaction is supported by the observation that the presence of inhibitors of cytochrome P-450, in particular of carbon monoxide, markedly decreased the rate of N-demethylation. Carbon Monoxide 162-177 cytochrome P-450 Oryctolagus cuniculus 127-143 3630202-12 1987 The direct involvement of cytochrome P-450 in the N-hydroxylation of benzamidine is supported by the observation that inhibitors of cytochrome P-450, in particular carbon monoxide, markedly decreased the rate of N-oxygenation. Carbon Monoxide 164-179 cytochrome P-450 Oryctolagus cuniculus 26-42 3630202-12 1987 The direct involvement of cytochrome P-450 in the N-hydroxylation of benzamidine is supported by the observation that inhibitors of cytochrome P-450, in particular carbon monoxide, markedly decreased the rate of N-oxygenation. Carbon Monoxide 164-179 cytochrome P-450 Oryctolagus cuniculus 132-148 6766934-3 1980 The carbon monoxide difference spectrum of the cytochrome P-450 fraction showed a maximum peak at 450 nm. Carbon Monoxide 4-19 cytochrome P-450 Oryctolagus cuniculus 47-63 7390994-3 1980 The reconstituted activity was sensitive to carbon monoxide, metyrapone, phenyl isocyanide, and cyanide, indicating that the cytochrome P-450 used is cyanide-sensitive and is involved in the catalytic process. Carbon Monoxide 44-59 cytochrome P-450 Oryctolagus cuniculus 125-141 6102025-2 1980 In addition to these quantitative changes, alterations in the nature of the type I and type II spectral interactions of substrates with hepatic cytochrome P-450 occurred during development, as did changes in the sensitivity of the hepatic mixed-function oxidase system to the inhibitory effects of carbon monoxide and SKF 525-A. Carbon Monoxide 298-313 cytochrome P-450 Oryctolagus cuniculus 144-160 113393-4 1979 The inhibition of the hydroxylation by SKF 525-A and carbon monoxide suggested that the activity depended upon cytochrome P-450. Carbon Monoxide 53-68 cytochrome P-450 Oryctolagus cuniculus 111-127