paper.edu.cn MINI-REVIEW Yin Li . Gongyuan Wei . Jian Chen Glutathione: a review on biotechnological production Received: 1 June 2004 / Revised: 16 August 2004 / Accepted: 31 August 2004 / Published online: 12 October 2004 # Springer-Verlag 2004 Abstract This Mini-Review summarizes the historic developments and technological achievements in the biotechnological production of glutathione in the past 30 years. Glutathione is the most abundant non-protein thiol compound present in living
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Foreign Literature Tobias Dick‚ researcher at the German Cancer Research Center‚ found that cells can produce their own anti-oxidants - glutathione - which fight off oxidants. According to Hagen‚ research on the natural processes of aging‚ and steps that could slow it or improve health until near the end of life‚ are of growing importance. Low glutathione levels‚ according to anti-aging research from the New England Journal of Medicine‚ can increase the risk of a heart attack. Dr. Eric Topol
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9. Summary and Conclusion ¬¬¬¬¬¬¬¬¬¬¬¬ 9.1 Herbal drugs are economical and their sources are plenty in India. As many synthetic show adverse effects. Attention of the healthcare practioners is directed towards herbal formulations to treat diseases with safety‚ effectiveness and stability. Majority of Indian population have the access to practice traditional or herbal medicines. Acacia catechu Willd. (family: Fabaceae) known as Black Cutch is used in traditional medical system for various diseases
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oxidation of glucose-6-phosphate to 6-phosphogluconate while also reducing NADP+ to NADPH‚ which is a required cofactor in many biosynthetic reactions. NADPH maintains glutathione in its reduced form that serves as a forager for hazardous oxidative metabolites in cells. With the help of the enzyme glutathione peroxidase‚ reduced glutathione also converts dangerous hydrogen peroxide to H20. Erythrocytes depend on G6PD activity since it is their only source of NADPH. Consequently‚ people lacking G6PD
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Acetaminophen Toxicity 1. Drug metabolizing enzymes convert acetaminophen to a reactive metabolite that bound to proteins covalently 2. Glutathione detoxify the metabolite and form acetaminophen-glutathione conjugate at nontoxic dose. However‚ the metabolite depleted hepatic glutathione and covalently bound to protein at toxic dose. Since diethylmaleate depleted hepatic glutathione without
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How taking extra Vitamin C lightens skin |In healthy adults‚ Vitamin C raises glutathione levels in the red blood cells and lymphocytes | |Glutathione helps determine the balance of light and dark pigments (pheomelanin and eumelanin) in our skin. L-cysteine and | |the TYRP1 enzyme also play a part in this balance | |Taking high doses of Vitamin C (1‚000 – 3‚000 mgs) can help to lighten skin
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Introduction Methionine and cysteine are both sulphur containing amino acids. Most proteins will contain one‚ or both of them at some point in the polypeptide chain. As such‚ many amino acids contain sulphur in some form‚ which is required in small amounts in the mammalian diet. Methionine has a thioether side chain‚ and cysteine’s contains a thiol group. These side chains exist as free thiols inside the cell‚ and are oxidised causing them to pair up and form disulphide bonds in an extracellular
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with the reduction of fat metabolism. Capability of enhancing memory Total alkaloid extracts of Murrya koenigii leaves‚ in doses of 20 and 40 mg/kg p.o.‚ improves the values of protective antioxidants like catalase‚ glutathione peroxidase‚ glutathione reductase‚ reduced glutathione and superoxide dismutase in brain homogenates. An increase in the acetylcholine levels and decrease in anticholinesterase activity has also been noticed. Thus‚ these properties play a beneficial role in protection against
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effect on aflatoxin accumulation. (2010). Oxidative stress and aging: is methylglyoxal the hidden enemy? Canadian Journal of Physiology and Pharmacology‚ 88‚ 3‚ 273-284‚ ISSN 1205-7541 Dixit‚ P.‚ Mukherjee‚ P.K.‚ Ramachandran‚ V. & Eapen‚ S. (2011). Glutathione transferase from Trichoderma virens enhances cadmium tolerance without enhancing its Eltayeb‚ A.E.‚ Kawano‚ N.‚ Badawi‚ G.‚ Kaminaka‚ H.‚ Sanekata‚ T. & Morishima‚ I. (2006). S. & Tanaka‚ K. (2007). Overexpression of monodehydroascorbate reductase
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B) Site of synthesis: 1- In pancreas: Synthesis of taurine in the mammalian pancreas occurs through the cysteine sulfinic acid pathway. First‚ in this pathway is oxidation of cysteine sulfahydryl group to sulfonic acid‚ this oxidation is catalyzed by the enzyme cysteine dioxygenase. In turn‚ cysteine sulfonic acid is decarboxylated to hypotaurine by sulfonoalanine decarboxylase. It is not well known whether hypotaurine is then enzymatically or spontaneously oxidized to taurine. 2- in CNS: Biosynthesis
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