PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1328604-7 1992 Furthermore, MB induced a dose- and time-dependent generation of superoxide anion from RPASM, as evidenced from spectrophotometric determination of cytochrome c reduction. Superoxides 65-81 LOC104968582 Bos taurus 148-160 2174293-3 1990 The production of superoxide was measured by the superoxide dismutase inhibitable reduction of cytochrome c. Superoxides 18-28 LOC104968582 Bos taurus 95-107 15389975-3 2004 Superoxide anion radicals were detected explosively in the extracellular space at 2-5 min after Reox following the Anox treatment of HUVE endotheliocytes, and were thereafter retained at levels as high as approximately one-half of the maximum level until 60 min after Reox, as shown by cytochrome c reduction assay. Superoxides 0-25 LOC104968582 Bos taurus 286-298 164898-0 1975 The role of superoxide radical in the autoxidation of cytochrome c. Superoxides 12-30 LOC104968582 Bos taurus 54-66 20933223-0 2010 Maillard reaction of ribose 5-phosphate generates superoxide and glycation products for bovine heart cytochrome c reduction. Superoxides 50-60 LOC104968582 Bos taurus 101-113 20933223-2 2010 In a reaction with the lysines of bovine heart cytochrome c, R5P generates superoxide (O2-) that subsequently reduces ferri-cytochrome c to ferro-cytochrome c. Superoxides 75-85 LOC104968582 Bos taurus 47-59 20933223-2 2010 In a reaction with the lysines of bovine heart cytochrome c, R5P generates superoxide (O2-) that subsequently reduces ferri-cytochrome c to ferro-cytochrome c. Superoxides 75-85 LOC104968582 Bos taurus 124-136 20933223-2 2010 In a reaction with the lysines of bovine heart cytochrome c, R5P generates superoxide (O2-) that subsequently reduces ferri-cytochrome c to ferro-cytochrome c. Superoxides 75-85 LOC104968582 Bos taurus 124-136 20933223-2 2010 In a reaction with the lysines of bovine heart cytochrome c, R5P generates superoxide (O2-) that subsequently reduces ferri-cytochrome c to ferro-cytochrome c. Superoxides 87-89 LOC104968582 Bos taurus 47-59 20933223-2 2010 In a reaction with the lysines of bovine heart cytochrome c, R5P generates superoxide (O2-) that subsequently reduces ferri-cytochrome c to ferro-cytochrome c. Superoxides 87-89 LOC104968582 Bos taurus 124-136 20933223-2 2010 In a reaction with the lysines of bovine heart cytochrome c, R5P generates superoxide (O2-) that subsequently reduces ferri-cytochrome c to ferro-cytochrome c. Superoxides 87-89 LOC104968582 Bos taurus 124-136 20933223-4 2010 The addition of amines to the cytochrome c-R5P system greatly increases the O2- generation with rates of approximately 1.0 muMmin(-1) being observed with millimolar levels of R5P and amine at 37 C. Pre-incubation of R5P with the amine prior to cytochrome c addition further enhances the rate of cytochrome c reduction approximately twofold for every 30 min of incubation. Superoxides 76-78 LOC104968582 Bos taurus 30-42 20933223-4 2010 The addition of amines to the cytochrome c-R5P system greatly increases the O2- generation with rates of approximately 1.0 muMmin(-1) being observed with millimolar levels of R5P and amine at 37 C. Pre-incubation of R5P with the amine prior to cytochrome c addition further enhances the rate of cytochrome c reduction approximately twofold for every 30 min of incubation. Superoxides 76-78 LOC104968582 Bos taurus 244-256 20933223-4 2010 The addition of amines to the cytochrome c-R5P system greatly increases the O2- generation with rates of approximately 1.0 muMmin(-1) being observed with millimolar levels of R5P and amine at 37 C. Pre-incubation of R5P with the amine prior to cytochrome c addition further enhances the rate of cytochrome c reduction approximately twofold for every 30 min of incubation. Superoxides 76-78 LOC104968582 Bos taurus 244-256 20933223-5 2010 While clearly accounting for a portion of the reduction of cytochrome c, O2- is not the sole reductant of the system as the use of superoxide dismutase only partially limits cytochrome c reduction, and the contribution of O2- proportionally decreases with longer amine-R5P incubation times. Superoxides 73-75 LOC104968582 Bos taurus 59-71 30812210-1 1979 Superoxide dismutase activity was shown to be present in bovine milk serum and was quantified by measuring the capacity of retentate from dialyzed milk serum to inhibit reduction of cytochrome c by xanthine-xanthine oxidase-generated superoxide anion. Superoxides 234-250 LOC104968582 Bos taurus 182-194 14700542-4 2004 In the classical assays, bactericidal effect on opsonized, live bacteria was quantified by the conversion of an indicator substance, superoxide anion production was assayed by the reduction of cytochrome c, whereas myeloperoxidase activity was determined with a radioactive iodination assay. Superoxides 133-149 LOC104968582 Bos taurus 193-205 11455018-8 2001 CYP2J2 transfection attenuated the HR-induced increase in 8-iso-prostaglandin F(2alpha) (p < 0.05) and decreased the amount of extracellular superoxide detected by cytochrome c reduction under normoxic conditions (p < 0.05) but did not significantly affect HR-induced decreases in eNOS expression, L-arginine uptake and conversion, and nitrite production. Superoxides 144-154 LOC104968582 Bos taurus 167-179 12429571-4 2002 Exposure to veratridine (30 micro M, 1 h) produces cytochrome c release to the cytoplasm that seems to be mediated by superoxide anions and that is blocked by cyclosporin A (10 micro M), MnTBAP (10 nM), catalase (100 IU ml(-1)) and vitamin E (50 micro M). Superoxides 118-135 LOC104968582 Bos taurus 51-63 12429571-17 2002 In conclusion, superoxide anions seem to mediate veratridine-induced cytochrome c release, decrease in total glutathione, caspase activation and cell death in bovine chromaffin cells. Superoxides 15-32 LOC104968582 Bos taurus 69-81 12429571-0 2002 Superoxide anions mediate veratridine-induced cytochrome c release and caspase activity in bovine chromaffin cells. Superoxides 0-17 LOC104968582 Bos taurus 46-58 11943469-3 2002 Treatment of SMP with X/XO resulted in a large production of superoxide anion, detected by acetylated cytochrome c method, which was blocked by superoxide dismutase (SOD). Superoxides 61-77 LOC104968582 Bos taurus 102-114 9852050-0 1998 Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria. Superoxides 14-30 LOC104968582 Bos taurus 44-56 11020659-0 2000 Detection of superoxide anion released extracellularly by endothelial cells using cytochrome c reduction, ESR, fluorescence and lucigenin-enhanced chemiluminescence techniques. Superoxides 13-29 LOC104968582 Bos taurus 82-94 10501655-3 1999 In agreement with the flow-cytometric findings, the inhibition of superoxide production was more important for SOD-pretreated monocytes than for neutrophils, as demonstrated with the cytochrome c reduction assay. Superoxides 66-76 LOC104968582 Bos taurus 183-195 10501655-7 1999 Superoxide production by monocytes and neutrophils was measured with the cytochrome c assay. Superoxides 0-10 LOC104968582 Bos taurus 73-85 8628756-6 1996 Superoxide anion attained a level of 76 microM as determined by the superoxide dismutase (SOD)-dependent increase in hydrogen peroxide formation and of 52 microM by the SOD-inhibitable reduction of cytochrome c. Superoxides 0-16 LOC104968582 Bos taurus 198-210 9223231-7 1997 Production of superoxide radicals measured by the cytochrome c reduction assay was lowered by danofloxacin, penicillin and chloramphenicol. Superoxides 14-24 LOC104968582 Bos taurus 50-62 9630350-2 1998 A number of superoxide dismutase (SOD) mimetics were examined both biochemically for their ability to inhibit the superoxide-catalyzed reduction of cytochrome c and nitro blue tetrazolium, and functionally for their ability to mimic authentic Cu/Zn SOD in restoring nitrergic neurotransmission in bovine retractor penis (BRP) muscle following its inhibition by oxidant stress. Superoxides 12-22 LOC104968582 Bos taurus 148-160 8846270-4 1996 Superoxide, hydrogen peroxide and hydroxyl radical formation was measured by superoxide dismutase-inhibitable cytochrome c reduction, the dichlorofluorescin technique and the salicylate method, respectively. Superoxides 0-10 LOC104968582 Bos taurus 110-122