Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-90 |
Sentence |
denotes |
Kinetic studies on the removal of extracellular hydrogen peroxide by cultured fibroblasts. |
T2 |
91-238 |
Sentence |
denotes |
To investigate the function of antioxidant enzymes in intact cells, we examined the removal of extracellular H2O2 by cultured fibroblasts (IMR-90). |
T3 |
239-406 |
Sentence |
denotes |
H2O2 concentration dependence of the reaction rate was interpreted as that the process involves two kinetically different reactions (referred to as reactions 1 and 2). |
T4 |
407-554 |
Sentence |
denotes |
Reaction 1 was characterized by a relatively low Km value (about 40 microM), and reaction 2 by linear dependence of the rate up to 500 microM H2O2. |
T5 |
555-734 |
Sentence |
denotes |
The magnitude of reaction 1 was reduced by treatment of the cells with diethyl maleate or 6-amino-nicotinamide, while reaction 2 was inhibited by 3-amino-1,2,4-triazole treatment. |
T6 |
735-840 |
Sentence |
denotes |
It was concluded that reactions 1 and 2 are principally due to GSH peroxidase and catalase, respectively. |
T7 |
841-1026 |
Sentence |
denotes |
The values of kinetic parameters were estimated by curve-fitting, and it was inferred that 80 to 90% of H2O2 is decomposed by GSH peroxidase at H2O2 concentrations lower than 10 microM. |
T8 |
1027-1106 |
Sentence |
denotes |
The contribution of catalase increases with the increase in H2O2 concentration. |
T9 |
1107-1229 |
Sentence |
denotes |
The intact cells showed a low catalase activity (about 15%), as compared with the activity found in the solubilized cells. |
T10 |
1230-1336 |
Sentence |
denotes |
The low catalase activity was ascribed to the latency of the enzyme caused by localization in peroxisomes. |
T11 |
1337-1404 |
Sentence |
denotes |
Fibroblasts also removed intracellular H2O2 generated by menadione. |
T12 |
1405-1521 |
Sentence |
denotes |
Treatment with diethyl maleate greatly impaired the H2O2-removing capability and caused H2O2 efflux into the medium. |
T1 |
0-90 |
Sentence |
denotes |
Kinetic studies on the removal of extracellular hydrogen peroxide by cultured fibroblasts. |
T2 |
91-238 |
Sentence |
denotes |
To investigate the function of antioxidant enzymes in intact cells, we examined the removal of extracellular H2O2 by cultured fibroblasts (IMR-90). |
T3 |
239-406 |
Sentence |
denotes |
H2O2 concentration dependence of the reaction rate was interpreted as that the process involves two kinetically different reactions (referred to as reactions 1 and 2). |
T4 |
407-554 |
Sentence |
denotes |
Reaction 1 was characterized by a relatively low Km value (about 40 microM), and reaction 2 by linear dependence of the rate up to 500 microM H2O2. |
T5 |
555-734 |
Sentence |
denotes |
The magnitude of reaction 1 was reduced by treatment of the cells with diethyl maleate or 6-amino-nicotinamide, while reaction 2 was inhibited by 3-amino-1,2,4-triazole treatment. |
T6 |
735-840 |
Sentence |
denotes |
It was concluded that reactions 1 and 2 are principally due to GSH peroxidase and catalase, respectively. |
T7 |
841-1026 |
Sentence |
denotes |
The values of kinetic parameters were estimated by curve-fitting, and it was inferred that 80 to 90% of H2O2 is decomposed by GSH peroxidase at H2O2 concentrations lower than 10 microM. |
T8 |
1027-1106 |
Sentence |
denotes |
The contribution of catalase increases with the increase in H2O2 concentration. |
T9 |
1107-1229 |
Sentence |
denotes |
The intact cells showed a low catalase activity (about 15%), as compared with the activity found in the solubilized cells. |
T10 |
1230-1336 |
Sentence |
denotes |
The low catalase activity was ascribed to the latency of the enzyme caused by localization in peroxisomes. |
T11 |
1337-1404 |
Sentence |
denotes |
Fibroblasts also removed intracellular H2O2 generated by menadione. |
T12 |
1405-1521 |
Sentence |
denotes |
Treatment with diethyl maleate greatly impaired the H2O2-removing capability and caused H2O2 efflux into the medium. |