نتایج جستجو برای: zn superoxide

تعداد نتایج: 70211  

Journal: :Plant physiology 1992
J J Burke M J Oliver

The activity of pea (Pisum sativum L.) Cu/Zn and Mn superoxide dismutase isoforms was evaluated across a range of temperatures from 10 to 45 degrees C. Maximal activity of the Cu/Zn and Mn superoxide dismutase isoforms was observed at 10 degrees C. Both cytoplasmic and chloroplast Cu/Zn superoxide dismutases exhibit a reduction in staining intensity with increasing temperatures. Mn superoxide d...

Journal: :Chemical communications 2015
Hanping Zhang Tao Yang Xin Wu Yisen Zhou Chao Yang Tian Zhu Rulin Dong

We propose an aqueous rechargeable Zn-Cu Daniell-type battery. In this system, Li(+) prefers to conduct currents rather than react with the electrodes, while the Zn-Cu electrode couples engage in their electrochemical reactions free from conducting currents. Here Li(+) performs like a messenger and thus could be called the electrochemical messenger.

1987
MIRJAM CVETIC

We discuss the structure of the effective Lagrangian for the (2,2) ZN orbifolds and the corresponding Calabi-Yau manifolds which are obtained by “blowing-up” the orbifold singularities. The method to “blow-up” such singularities is reviewed.’ Results are exact at the string tree-level. In particular the question of generating an intermediate scale MI in such models is addressed. It is shown tha...

Journal: :Biochemical Society transactions 2003
A Desideri M Falconi

The Cu,ZnSODs (Cu,Zn superoxide dismutases) comprise a class of ubiquitous metalloenzymes that catalyse the dismutation of the superoxide radical anion into oxygen and hydrogen peroxide. The dismutation reaction involves two successive encounters of the superoxide anion with a catalytic copper centre hosted by the enzyme at the dead end of a narrow protein channel. Cu,ZnSOD is found in all euka...

Journal: :Biochemical Society transactions 2003
A Battistoni

Several bacterial pathogens possess sodC genes that encode periplasmic or membrane-associated Cu,Zn superoxide dismutases. Since professional phagocytes generate large amounts of reactive oxygen species to control the growth of invading micro-organisms, Cu,Zn superoxide dismutase might protect infectious bacteria from oxy-radical damage and facilitate their survival within the host. This idea h...

1994
Lin X. Chen Zhiyu Wang Gerhard Hartwich Hugo Scheer Avigdor Scherz Pedro A. Montano James R. Norris

Local structures around metal atoms in Hi and Zn substituted 132-hydroxy-bacteriochlorophyll a (Ni-HOB, and Zn-HOB) with and without insertion into the accessory bacteriochlorophyll a (BChla) sites in Rhodobacter sphaeroides photosynthetic reaction centers (RC) are studied using X-ray absorption spectroscopy. The penta-coordination of Ni-HOB and Zn-HOB in the RC is similar to that of BChl a in ...

Journal: :The Biochemical journal 2005
Pedro Iñarrea Hadi Moini Daniel Rettori Derick Han Jesús Martínez Inés García Erika Fernández-Vizarra María Iturralde Enrique Cadenas

The localization of Cu,Zn-superoxide dismutase in the mitochondrial intermembrane space suggests a functional relationship with superoxide anion (O2*-) released into this compartment. The present study was aimed at examining the functionality of Cu,Zn-superoxide dismutase and elucidating the molecular basis for its activation in the intermembrane space. Intact rat liver mitochondria neither sca...

Journal: :The Journal of biological chemistry 1992
G S Dhaunsi S Gulati A K Singh J K Orak K Asayama I Singh

In this study, by using highly purified rat liver peroxisomes, we provide evidence from analytical cell fractionation, Western blot, and immunocytochemical analysis that Cu-Zn superoxide dismutase is present in animal peroxisomes. Treatment with ciprofibrate, a peroxisome proliferator, increased the peroxisomal superoxide dismutase activity by 3-fold with no effect on mitochondrial activity but...

Journal: :Infection and immunity 1998
K E Wilks K L Dunn J L Farrant K M Reddin A R Gorringe P R Langford J S Kroll

Meningococcal sodC encodes periplasmic copper- and zinc-cofactored superoxide dismutase (Cu,Zn SOD) which catalyzes the conversion of the superoxide radical anion to hydrogen peroxide, preventing a sequence of reactions leading to production of toxic hydroxyl free radicals. From its periplasmic location, Cu,Zn SOD was inferred to acquire its substrate from outside the bacterial cell and was spe...

2017
Yuya Nakamura Masahiro Inagaki Sachiyo Kenmotsu Shiho Yamadera Isao Ohsawa Hiromichi Gotoh Yoshikazu Goto Naoki Sato Tatsunori Oguchi Mayumi Tsuji Yuji Kiuchi

Cu/Zn-superoxide dismutase (Cu/Zn-SOD) is an enzyme that is ubiquitously present in the cytoplasm and causes dismutation of superoxide radicals, therefore Cu/Zn-SOD is primarily used as an antioxidant marker. Levels of Cu/Zn-SOD are higher in the serum of hemodialysis patients than in serum of healthy volunteers. The increase of serum Cu/Zn-SOD levels is related to the decrease of kidney functi...

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