نتایج جستجو برای: superoxide
تعداد نتایج: 33639 فیلتر نتایج به سال:
Superoxide production by stimulated neutrophils and by preparations of NADPH oxidase has consistently been measured by an indirect method utilising the reduction of cytochrome c by superoxide radicals [4]. This reduction is inhibited by superoxide dismutase. EPR spectroscopy using the technique of spin trapping has been used to identify superoxide radicals formed by photo-irradiated spinach chl...
Inhibition of tumor necrosis factor-alpha (TNFα) and superoxide anion production reduces inflammation and pain. The present study investigated whether superoxide anion-induced pain depends on TNFα signaling and the role of superoxide anion in TNFα-induced hyperalgesia to clarify the interrelation between these two mediators in the context of pain. Intraplantar injection of a superoxide anion do...
Nitric oxide and superoxide have important roles as vascular signaling molecules. Nitric oxide (NO) reacts rapidly with superoxide, producing peroxynitrite. The relative balance between these radicals has important implications for vascular pathophysiology in hypertension and other vascular disease states. However, the relationships between superoxide, NO, and peroxynitrite formation in human b...
Photosynthetic oxygen reduction by isolated chloroplast lamellar systems has been studied with the aid of superoxide dismutase. Two mechanisms of oxygen reduction by illuminated chloroplast lamellar systems can be differentiated: 1. In the presence of low potential electron acceptors like AQ or MV the superoxide free radical ion is the product of autooxidation of the reduced acceptor. Addition ...
Partially purified soluble rat liver guanylate cyclase [GTP pyrophosphate-lyase (cyclizing), EC 4.6.1.2] was activated by superoxide dismutase (superoxide: superoxide oxidoreductase, EC 1.15.1.1). This activation was prevented with KCN or glutathione, inhibitors of superoxide dismutase. Guanylate cyclase preparations formed superoxide ion. Activation by superoxide dismutase was further enhanced...
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