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| Content Provider | Springer Nature Link |
|---|---|
| Author | Sazontova, T. G. Guseva, N. V. Lisitsina, T. A. Arkhipenko, Yu. V. Durnev, A. D. |
| Copyright Year | 1997 |
| Abstract | Catalase and superoxide dismutase activities in the liver of NZW mice are 29.3 μmol H2O2/min×mg protein and 10.6 U/mg protein, respectively. The rate of accumulation of lipid peroxidation (LPO) products is low within the first 60 min of incubation of liver homogenates with ascorbate and then rapidly increases. A similar process is observed with Fe+ascorbate system, where LPO rate is markedly higher and lag-period lasts 10 min. Under the action of cyclophosphane the activity of catalase increases by 32%, while that of superoxide dismutase decreases by 46%, which is accompanied by a decline in the sensitivity of liver tissue to LPO induction. When LPO is inducedin vitro by ascorbate, lag-period decreases 2-fold, while the rate of accumulation of LPO products increases by 38% and their maximum level by 35% compared with the control. Similar processes develop in the Fe+ascorbate system. Dioxydine induces no significant changes in the activities of catalase and superoxide dismutase as well as in LPO product accumulation in the ascorbate and Fe+ascorbate systems. |
| Starting Page | 328 |
| Ending Page | 330 |
| Page Count | 3 |
| File Format | |
| ISSN | 00074888 |
| Journal | Bulletin of Experimental Biology and Medicine |
| Volume Number | 123 |
| Issue Number | 4 |
| e-ISSN | 15738221 |
| Language | English |
| Publisher | Springer US |
| Publisher Date | 1997-01-01 |
| Publisher Place | Boston |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | lipid peroxidation superoxide dismutase catalase dioxydine cyclophosphane NZW mice Biomedicine general Internal Medicine Cell Biology Pathology Laboratory Medicine |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Biochemistry, Genetics and Molecular Biology |
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