scholarly journals Effect of Anthelmintics on Antioxidant Enzymes in Arabidopsis Thaliana

Author(s):  
Radka Podlipná ◽  
Eliška Syslová ◽  
Markéta Hanulíková ◽  
Lucie Raisová Stuchlíková ◽  
Barbora Szotáková ◽  
...  
2016 ◽  
Vol 63 (6) ◽  
pp. 749-753 ◽  
Author(s):  
M. S. Sin’kevich ◽  
A. A. Selivanov ◽  
O. V. Antipina ◽  
E. V. Kropocheva ◽  
G. P. Alieva ◽  
...  

2018 ◽  
Vol 15 (2) ◽  
pp. 138-144
Author(s):  
I. M. Buzduga ◽  
R. A. Volkov ◽  
I. I. Panchuk

Aim. To better understand the mechanisms of abiotic stress resistance in plants, it is important to clarify the role of individual antioxidant enzymes from the same multiproteinic family in the response to stress. It is known that the loss of some isoforms of antioxidant enzymes can be compensated by activation of other enzymes. However, the functional interaction of the ascorbate-glutathione cycle enzymes with catalase under salt stress still remains unexplored. Respectively, we determined the activity of DHAR in knock-out mutants of Arabidopsis thaliana under salt stress. Methods. The DHAR activity was determined in the knock-out line cat2 and in wild-type (WT) Arabidopsis plants after various regimes of treatment with sodium chloride. Results. After treatment with 200 mM sodium chloride in the dark, activation of DHAR was found after 8 hours in WT plants and after 4 hours in the knock-out line cat2. However stress treatment under illumination resulted in significant increase in DHAR activity after 8 hours in both studied lines. In this case, DHAR activity in cat2 was lower than in WT, whereas in non-treated plants or upon stress treatment in the dark no difference between the tested lines was detected. Conclusions. The obtained data indicate that under salt stress conditions, changes in the DHAR activity are included into functional rearrangements of the antioxidant system in cat2 line, which compensate the loss of activity of CAT2 isoenzyme.Keywords: dehydroascorbate reductase, antioxidants, reactive oxygen species (ROS), salt stress, Arabidopsis thaliana


Author(s):  
Ye Yang ◽  
Wenguang Cai ◽  
Junchao Wang ◽  
Weimin Pan ◽  
Lin Liu ◽  
...  

Peroxiredoxins (Prxs), a large family of antioxidant enzymes, are abundant in all living organisms. Peroxiredoxin A (PrxA) from Arabidopsis thaliana belongs to the typical 2-Cys Prx family and is localized in the chloroplast. This article reports the crystal structure of a PrxA C119S mutant refined to 2.6 Å resolution. The protein exists as a decamer both in the crystal structure and in solution. The structure is in the reduced state suitable for the approach of peroxide, though conformational changes are needed for the resolving process.


2010 ◽  
Vol 73 (6) ◽  
pp. 1362-1369 ◽  
Author(s):  
Maria Drążkiewicz ◽  
Ewa Skórzyńska-Polit ◽  
Zbigniew Krupa

2008 ◽  
Vol 9 (1) ◽  
pp. 44-50 ◽  
Author(s):  
A. Saffar ◽  
M.B. Bagherieh ◽  
M. Mianabadi

1999 ◽  
Vol 112 (3) ◽  
pp. 279-290 ◽  
Author(s):  
Akihiro Kubo ◽  
Mitsuko Aono ◽  
Nobuyoshi Nakajima ◽  
Hikaru Saji ◽  
Kiyoshi Tanaka ◽  
...  

1994 ◽  
Vol 5 (4) ◽  
pp. 551-558 ◽  
Author(s):  
Seok So Chang ◽  
Soon Ki Park ◽  
Byung Chul Kim ◽  
Bong Joong Kang ◽  
Dal Ung Kim ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document