نتایج جستجو برای: Glutathione disulfide (GSSG)

تعداد نتایج: 57687  

Journal: :iranian journal of pharmaceutical research 0
zahra hami 1- department of pharmacology, school of medicine, tehran university of medical sciences, tehran, iran. 2- department of medical nanotechnology, school of advanced technologies in medicine, tehran university of medical sciences, tehran, iran. mohsen amini department of medicinal chemistry, faculty of pharmacy and drug design and development research center, university of medical sciences, tehran, iran. amir kiani department of pharmacology, toxicology and medical services, school of pharmacy, kermanshah university of medical sciences, kermanshah, iran. mahmoud ghazi-khansari department of pharmacology, school of medicine, tehran university of medical sciences, tehran, iran.

glutathione (gsh) is one of the most important antioxidants that plays an essential role in detoxification of reactive oxygen species (ros) which oxidizes to glutathione disulfide (gssg). paraquat (pq), awidely used herbicide, causes pulmonary injury with the productionof ros. excessive ros accumulation as a consequence of pq exposure are frequently targeted by gsh thereby oxidative stress lead...

Glutathione (GSH) is one of the most important antioxidants that plays an essential role in detoxification of reactive oxygen species (ROS) which oxidizes to glutathione disulfide (GSSG). Paraquat (PQ), awidely used herbicide, causes pulmonary injury with the productionof ROS. Excessive ROS accumulation as a consequence of PQ exposure are frequently targeted by GSH thereby oxidative stress lead...

Glutathione (GSH) is one of the most important antioxidants that plays an essential role in detoxification of reactive oxygen species (ROS) which oxidizes to glutathione disulfide (GSSG). Paraquat (PQ), awidely used herbicide, causes pulmonary injury with the productionof ROS. Excessive ROS accumulation as a consequence of PQ exposure are frequently targeted by GSH thereby oxidative stress lead...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1999
J K Suh L L Poulsen D M Ziegler J D Robertus

The flavin-containing monooxygenase from yeast (yFMO) catalyzes the O2- and NADPH-dependent oxidations of biological thiols, including oxidation of glutathione to glutathione disulfide (GSSG). Glutathione and GSSG form the principle redox buffering system in the cell, with the endoplasmic reticulum (ER) being more oxidizing than the cytoplasm. Proper folding of disulfide-bonded proteins in the ...

Journal: :The Journal of biological chemistry 1980
M Usami H Matsushita T Shimazu

The mechanism of inactivation of rabbit liver phosphorylase phosphatase by glutathione disulfide (GSSG) was investigated. The catalytic subunit of phosphorylase phosphatase was inactivated by GSSG and other disulfides. Inactivation by GSSG was a concentration-dependent process and resulted in the formation of an inactive, stable enzyme species. The inactivated enzyme could be reactivated by add...

2013
Zahra Hami Mohsen Amini Amir Kiani Mahmoud Ghazi-Khansari

Glutathione (GSH) is one of the most important antioxidants that plays an essential role in detoxification of reactive oxygen species (ROS) which oxidizes to glutathione disulfide (GSSG). Paraquat (PQ), awidely used herbicide, causes pulmonary injury with the productionof ROS. Excessive ROS accumulation as a consequence of PQ exposure are frequently targeted by GSH thereby oxidative stress lead...

Journal: :Molecular & cellular proteomics : MCP 2006
Jonathan P Brennan Jonathan I A Miller William Fuller Robin Wait Shajna Begum Michael J Dunn Philip Eaton

Glutathione disulfide (GSSG) accumulates in cells under an increased oxidant load, which occurs during neurohormonal or metabolic stimulation as well as in many disease states. Elevated GSSG promotes protein S-glutathiolation, a reversible post-translational modification, which can directly alter or regulate protein function. We developed novel strategies for the study of protein S-glutathiolat...

Journal: :Acta biochimica Polonica 2011
Zahid M Delwar Marina Fernanda Vita Åke Siden Mabel Cruz Juan Sebastian Yakisich

In most cells, the major intracellular redox buffer is glutathione (GSH) and its disulfide-oxidized (GSSG) form. The GSH/GSSG system maintains the intracellular redox balance and the essential thiol status of proteins by thiol disulfide exchange. Topoisomerases are thiol proteins and are a target of thiol-reactive substances. In this study, the inhibitory effect of physiological concentration o...

2001
E. F.

In glutathione redox buffers, rat liver, microsomal 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase rapidly equilibrates between a reduced, active form and an oxidized, inactive form. At pH 7.0, 37 “C, the second order rate constant for inactivation of the reduced enzyme by GSSG is 1700 f 200 M-’ min-l, approximately 20-fold faster than the reaction of GSSG with a typical, unhindered ...

Journal: :The Journal of biological chemistry 1986
D W Walters H F Gilbert

Chicken liver fatty acid synthase is rapidly inactivated and cross-linked at pH 7.2 and 8.0 by incubation with low concentrations of common biological disulfides including glutathione disulfide, coenzyme A disulfide, and glutathione-coenzyme A-mixed disulfide. Glutathione disulfide inactivation of the enzyme is accompanied by the oxidation of a total of 4-5 enzyme thiols per monomer. Only one g...

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