• Supplementation with glutathione, a cysteine-containing antioxidative tripeptide, normalized hepatic glutathione redox state modulated by ingestion of 3% CN diet, but it only reversed the oxidized shift of plasma albumin redox state to an extent similar to cystine alone or the constituting amino acid mixture of glutathione (i.e., glutamic acid, cystine, and glycine), indicating that glutathione would primarily serve as a source of cysteine rather than exert its antioxidative activity. (frontiersin.org)
  • Immunotec's proprietary manufacturing process preserves the critical disulfide bonds in the glutathione precursor cysteine. (immunotec.com)
  • Cysteine, glutathione and albumin thiols reduced TETD with subsequent mixed disulfide formation suggesting a potential route of protein haptenation. (cdc.gov)
  • In response to reactive oxygen species (ROS), glutathione plays an important role in redox signaling by forming a disulfide bond with protein cysteine residues, known as glutathionylation. (thieme-connect.com)
  • Reducing agents cysteine, glutathione and dithiothreitol in the concentration range of 10 µM-10 mM diminished binding of [ 3 H]3-quinuclidinyl benzilate ([ 3 H]3-QNB) to in situ muscarinic receptor sites of membranes from rat cerebral cortex. (aspetjournals.org)
  • Cysteine is then metabolized to sulfite, taurine, and glutathione. (msdmanuals.com)
  • By delivering this delicate protein to the cell, it enables the body to create glutathione and maximize immune system levels. (immunotec.com)
  • Oxidation of ZDEC by bleach, iodine or hydrogen peroxide resulted in production of TETD, tetraethylthiocarbamoyl disulfide (TETCD) and tetraethyldicarbamoyl disulfide (TEDCD). (cdc.gov)
  • CoDEC does not bind to Cu-proteins or form mixed disulfides with free thiols demonstrating the importance of these properties in ZDEC sensitization. (cdc.gov)
  • It is concluded that ZDEC may haptenize proteins through (1) chelation of metals on metalloproteins, (2) TETD mediated formation of mixed disulfides, and (3) possibly through nucleophilic addition onto an TEDCD electrophilic carbamoyl group. (cdc.gov)
  • I was wondering if anyone has used a glutathione analog in which the sulfhydral group is blocked to elude bound GST-fusion proteins from a GSH-Sepharose Chromatography Column (Pharmacia). (bio.net)
  • Sulfur, in the form of disulfide bonds, provides strength and resiliency to hair, feathers, and feathered hair . (marksdailyapple.com)
  • Reduced glutathione (GSH) is currently used, but it binds to our peptides via two disulfide bonds to two cysteines in our target peptide. (bio.net)
  • Glycosaminoglycans are the building blocks of joint cartilage, and these molecules are connected with disulfide bonds (the bonding of two sulfur atoms). (springtimeinc.com)
  • AtSAL1 phosphatase activity is suppressed by dimerization, intramolecular disulfide formation, and glutathionylation, allowing accumulation of its substrate, PAP, a chloroplast stress retrograde signal that regulates expression of plastid redox associated nuclear genes (PRANGs). (nih.gov)
  • Reversible modification of cysteines such as disulfide bond formation, glutathionylation, and nitrosylation may also be a means of protection from further, generally irreversible, modifications to sulfinic (-SO 2 H) or sulfonic (-SO 3 H) acids [ 9 ]. (hindawi.com)
  • We briefly review the roles of glutathione, ROS, and glutathionylation in redox regulation. (thieme-connect.com)
  • Additionally, items such as milk, blueberries, bottled apple juice and tea contain glutathione-reactive compounds that reduce the amount of glutathione present in food or lining of the small intestine. (preparedfoods.com)
  • This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. (nih.gov)
  • 2006). The LLNA is based upon characterization of chemicals comprising allergens of different potencies and non- induced proliferative responses in draining lymph nodes allergenic chemicals were evaluated for their ability to react with following topical exposure of mice to chemicals (Gerberick reduced glutathione (GSH) or with two synthetic peptides et al. (cdc.gov)
  • Increased oxidant burden and antioxidant, e.g. glutathione (GSH), deficiency in the lower respiratory tract have been thought to play a role in the progression of IPF. (ersjournals.com)
  • Albumin with a free thiol on Cys34 is the reduced form and designated as mercaptalbumin (MA), while the isoforms with oxidized Cys34, such as a mixed disulfide with low molecular weight thiols and sulfinic/sulfonic acid, are the oxidized forms, which are designated as non-mercaptalbumin (NA)-1 and NA-2, respectively. (frontiersin.org)
  • Rate constants for the reaction of hydroxyl radicals with carbonyl sulfide, carbon disulfide and dimethyl thioether over the temperature range 299-430 K. (cdc.gov)
  • The other constituents of note are low molecular weight sulfur-containing constituents, dimethyl sulfide, dimethyl disulfide and methyl mercaptan, The Boundary Composition for the registration substance limits the total amount of sulfur-containing constituents to 6% by weight expressed as sulfur. (europa.eu)
  • For worker exposure, the approach used is to consider whole substance (based on pinene data) and sulfides (based on dimethyl disulfide data) (Section 9.0). (europa.eu)
  • The tripeptide glutathione (l-y-glutamyl-l-cysteinyl-glycine, GSH) plays a pivotal role in metabolic and cell-cycle related functions in virtually all cells. (ersjournals.com)
  • Ninety percent of glutathione in the cell exists in reduced form and 10% in oxidative form, and it typically acts as an antioxidant defense mechanism. (medscape.com)
  • Animal research with glutathione supplementation has indicated improvements in immune function, 2 protection against oxidant injury in newborn lungs, 3 reduction in the uptake of oxidized lipids 4 and protection against other toxic chemicals. (preparedfoods.com)
  • 5 Human research has shown that glutathione from raw fruits and vegetables is associated with a reduced risk of oral cancer 6 and supplementation with glutathione can prevent nephrotoxicity associated with cancer treatment. (preparedfoods.com)
  • 7 Clinical trials are needed to confirm glutathione supplementation and the proposed associated health benefits seen in animal studies. (preparedfoods.com)
  • We suspect that the cysteines form a native disulfide bond in the absence of GSH and DTT. (bio.net)
  • 1988. Neurological examination, computerized- tomography, cerebral blood-flow and neuropsychological examination in workers with long-term exposure to carbon disulfide. (cdc.gov)
  • Modification of thiol-disulfide state of receptor may be involved in the control of binding activity. (aspetjournals.org)
  • Research has indicated that supplemental glutathione results in increased plasma glutathione levels in humans, despite an expected degradation that may occur in the intestine. (preparedfoods.com)
  • 1985. Effect of carbon disulphide on the cardiovascular system. (cdc.gov)
  • Elevated levels of glutathione disulfide are associated with increased carotid intima media thickness, a measurement of the thickness of artery walls and an indication of cardiovascular disease risk. (preparedfoods.com)
  • Glutathione donates electrons to oxidants to sequester, or squelch, their free radical activity, helping to prevent DNA damage and subsequent chronic disease. (preparedfoods.com)
  • Zinc diethyldithiocarbamate (ZDEC) and its disulfide, tetraethylthiuram disulfide (TETD) are rubber accelerant contact allergens that cross-react in some individuals. (cdc.gov)
  • 1980. Measurements of emission rates of carbon disulfide from biogenic sources and its possible importance to the stratospheric aerosol layer. (cdc.gov)
  • Homocysteine accumulates and dimerizes to form the disulfide homocystine, which is excreted in the urine. (msdmanuals.com)
  • The results suggested that a disulfide bond, which could be reduced and reoxidized, may play an important role in ligand binding. (aspetjournals.org)