PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9193873-0 1997 Cytochrome P450 responsible for the stereoselective S-oxidation of flosequinan in hepatic microsomes from rats and humans. flosequinan 67-78 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 0-15 9193873-1 1997 The forms of cytochrome P450 involved in the stereoselective S-oxidation of flosequinan [(+/-)-7-fluoro-1-methyl-3-methylsulfinyl-4-quinolone] were investigated in vitro using liver microsomes from rats and humans. flosequinan 76-87 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 13-28 9193873-1 1997 The forms of cytochrome P450 involved in the stereoselective S-oxidation of flosequinan [(+/-)-7-fluoro-1-methyl-3-methylsulfinyl-4-quinolone] were investigated in vitro using liver microsomes from rats and humans. flosequinan 89-141 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 13-28 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. phenylalanylserine 94-96 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. r-fso 100-105 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. s-fso 119-124 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. r-fso 246-251 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. s-fso 256-261 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-8 1997 Anti-CYP3A2 antisera inhibited the activities of the S-oxidases catalyzing the reactions from FS to R-FSO (40%) and to S-FSO (60%) at the high substrate concentration and inhibited the activities of the S-oxidases, thus catalyzing reactions from R-FSO and S-FSO to FSO2 (70%) at both high and low substrate concentrations. fso2 265-269 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-9 1997 These results suggest that CYP3A is the major enzyme involved in all S-oxidation pathways in flosequinan metabolism in rats. flosequinan 93-104 cytochrome P450, family 3, subfamily a, polypeptide 62 Rattus norvegicus 27-32 9193873-11 1997 Anti-CYP3A2 antisera inhibited the activities of all the S-oxidases in human liver microsomes ranging from 40 to 80%, suggesting that CYP3A is also involved in all of the S-oxidations of flosequinan in humans. flosequinan 187-198 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 5-11 9193873-11 1997 Anti-CYP3A2 antisera inhibited the activities of all the S-oxidases in human liver microsomes ranging from 40 to 80%, suggesting that CYP3A is also involved in all of the S-oxidations of flosequinan in humans. flosequinan 187-198 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 5-10