A new spectrophotometric technique that was previously described by Erel and Neselioglu  was used to establish thiol/ disulfide
Increased levels of plasma LDL, as well as the disruption of this antioxidant system by disulfide
depletion, initiate the atherosclerotic process in the arterial wall.
The latter organisms lack the typical glutathione reductase (GR) and TR enzymes, and TGR is the only disulfide
reductase involved in the regeneration of the reduced state of both thioredoxin (trx) and glutathione.
Thiols engage in oxidation reactions with oxidant molecules, forming disulfide
Another approach for intrinsic self-healing is by means of the formation of covalent bonds that allow chain exchange reactions such as the dynamic reversible formation of acylhydrazones , trithiocarbonates reshuffling , the reaction exchange of siloxane segments [13, 14], and the metathesis reaction of disulfide
The vascular OxS observed in MetS leads to a change in plasma redox state, inciting a prooxidant environment due to the imbalance of two central thiol/disulfide couples, glutathione/glutathione disulfide
(GSH/GSSG), and cysteine/cystine (Cys/CySS) [25, 27].
Once it commits to the plasma cell stage, the TP cysteine is used, in fact, to covalently link [H.sub.2][L.sub.2] "monomeric" units in polymeric secretory IgM by disulfide
For the load of 5N, wear negative values were obtained for both commercial and nanolamellar molybdenum disulfides
. Supposedly, it can be explained that the wear track is "overclad" with copper nanoparticles at a lower friction load.
Trichloromethyl phythalimido disulfide
was prepared by the reaction of potassium phthalimide with trichloromethane thiosulfenyl chloride as shown in Scheme 3.
The major difference between them is that the disulfides
, the most modern of which is TTFD (Fig 1) is hydro-lyzed on contact with cell membranes and the open ring thiamine passes into the cell without requiring the physiological transport system.
During these experiments, we gained knowledge about the catalytic properties of the enzyme, which enabled us to construct an enzymic assay for homocysteine in rat and mouse tissues as well as in plasma from mice (1).When this methodological work was being carried out in 1982, data on homocysteine were sparse and addressed limited aspects of homocysteine in health and disease, such as homocyst(e)ine in patients with the inborn error of homocystinuria, increased homocyst(e)ine (often the homocysteine-cysteine mixed disulfide
) in patients with cardiovascular disease (CVD), and the so-called methionine dependence of some cancer cells (2).