Estimation of Mono-Dehydroascorbate Reductase (MDAR) Activity

Author(s):  
M. Senthilkumar ◽  
N. Amaresan ◽  
A. Sankaranarayanan
1997 ◽  
Vol 38 (2) ◽  
pp. 173-178 ◽  
Author(s):  
Y. Kato ◽  
J. Urano ◽  
Y. Maki ◽  
T. Ushimaru

2006 ◽  
Vol 52 (2) ◽  
pp. 89-95 ◽  
Author(s):  
Katsumi AMAKO ◽  
Takashi USHIMARU ◽  
Ayami ISHIKAWA ◽  
Yasuka OGISHI ◽  
Ritsuko KISHIMOTO ◽  
...  

FEBS Letters ◽  
2000 ◽  
Vol 466 (1) ◽  
pp. 107-111 ◽  
Author(s):  
Jun'ichi Urano ◽  
Tomofumi Nakagawa ◽  
Yasushi Maki ◽  
Takehiro Masumura ◽  
Kunisuke Tanaka ◽  
...  

2003 ◽  
Vol 33 (10) ◽  
pp. 1035-1042 ◽  
Author(s):  
Fabrizio Bruschi ◽  
Michela Saviozzi ◽  
Simona Piaggi ◽  
Gino Malvaldi ◽  
Alessandro Casini

2001 ◽  
Vol 20 (7) ◽  
pp. 373-376 ◽  
Author(s):  
G Aykaç-Toker ◽  
S Bulgurcuogélu ◽  
N Koçak-Toker

Glutaredoxin is an important enzyme in thiol homeostasis. As a thioltransferase, it reduces oxidized thiols. It also has dehydroascorbate reductase (DHAR) activity to reduce dehydroascorbate (DHA) to ascorbic acid. Peroxynitrite (ONOO-) is one of the most active elements of oxidative stress that can be formed wherever nitric oxide and superoxide are produced simultaneously. ONOO- is known to react with free thiols easily. To observe the effect of ONOO- on glutaredoxin, rat liver cytosolic fractions were incubated with 0–250 MONOO -. Thioltransferase activity was found to be decreased as ONOO- concentration increased. The inhibition was not reversible with dithiothreitol (DTT). In cytosol besides glutaredoxin, another enzyme with DHAR activity is also present. In our study, the cytosolic DHAR activity which consisted both enzymes, was also inhibited by ONOO-, but DTT was able to return the activity almost completely.


FEBS Letters ◽  
1998 ◽  
Vol 425 (3) ◽  
pp. 528-529 ◽  
Author(s):  
Christine H Foyer ◽  
Philip M Mullineaux

2009 ◽  
Vol 51 (11) ◽  
pp. 993-1001 ◽  
Author(s):  
Hai-Ling Yang ◽  
Ying-Ru Zhao ◽  
Cai-Ling Wang ◽  
Zhi-Ling Yang ◽  
Qing-Yin Zeng ◽  
...  

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