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Human serum albumin oxidation

The effect of P-carotene on human serum albumin oxidation by 2,2 -azobis (2-amidinopropane) dihydrochloride under 15,150, and 760 torr of O2 to form carbonyls was related to O2 tension, antioxidant concentrations and interaction between mixtures of antioxidants (Zhang and Omaye 2000). High concentration of P-carotene produced more protein oxidation in the presence of high O2 tension by a prooxidant mechanism. Mixtures of P-carotene, a-tocopherol and ascorbic acid provided better protective effects on protein oxidation than any single compound. [Pg.100]

Investigations of the effects of UV- and hypochlorite-induced oxidative modification of 20 amino acids and human serum albumin (HSA) on their antiradical properties showed unexpected results [36], Seven amino acids (cystine, histidine, methionine, phenylalanine, serine, tryptophan, and tyrosine) and HSA developed ACW following oxidation (see examples in Fig. 14). The fresh (produced in 1998) HSA from Serva had no antiradical capacity, but it acquired this quality during irradiation. The out-of-date HSA sample (Dessau, GDR, 1987, expiration date 7/1/1992) showed a remarkable ACW even in an unirradiated state. [Pg.516]

Ab, Antibody BBB, Blood Brain Barrier CNS, Central Nervous System HIV, Human Immunodeficiency Virus HSA, Human Serum Albumin IGF, Insulin Growth Factor I/R, Ischaemia/Reperfusion MW, Molecular Weight OxLDL, Oxidized Low Density Lipoprotein -R, -receptor sCD4, soluble CD4 VEGF, Vascular Endothelial Growth Factor. [Pg.373]

Cooper et al. [21, 22] reported in detail the results of their laborious work on the adsorption of four proteins human serum albumin (HSA), fibrinogen (FGN), fibronectin (FN), and vitronectin (VN), on five biomaterials polyethylene (PE), silicone rubber (SR), Teflon-FEP (FEP), poly(tetramethylene oxide)-poly-urethane (PTMO-PU), and polyethylene oxide)-polyurethane(PEO-PU). Hard segments of these polyurethanes are composed of a methylene-bis(p-phenylisocyanate) (MDI) chain extended wih 1,4-butanediol. [Pg.13]

Peroxynitrite is a nonspecific oxidant that reacts with all classes of biomolecules depleting low-molecular-weight antioxidants, initiating lipid peroxidation, damaging nucleic acids and proteins. Its reactions are much slower than those of the hydroxyl radical but are faster than those of hydrogen peroxide. Comparison of peroxynitrite reactivity with various amino acid residues of human serum albumin have shown that cysteine, methionine, and tryptophan are the most reactive... [Pg.184]

Human serum albumin coupled to Sepharose-entrapped iron oxide particles from a ferrofluid (108). [Pg.19]

Filipe P, Morliere P, Patterson LK, Hug GL, Maziere J-C, Freitas JP, Fernandes A, Santus R. (2004) Oxygen-copper (11) interplay in the repair of semi-oxidized urate by quercetin bound to human serum albumin. Free Radic Res 38 295-301. [Pg.593]

That c in faet reflects helical content is shown by its rise in proteins for which there is independent evidence that helical content is being increased. The nonaqueous transitions of insulin, native and oxidized ribonuclease, silk fibroin, and oxidized bovine serum albumin (Yang and Doty, 1957) as well as that for carboxymethylated human serum albumin (Bresler... [Pg.501]

DeMaster, E, G., Quast, S.) Red fern, and Nagasawa, H- T (1995). Reaction of nitric nside Avith the free sulfhydryl group of human serum albumin yields a sulfenic acid and nitrous oxide, Biochemislry 34,11494-11499. [Pg.676]

Fig. 9 The effect of residual water on the stability of freeze-dried proteins. Circles = human growth hormone deamidation and oxidation at 25° C, %/month squares = aggregation of human serum albumin at 50°C, %/day triangles = hemoglobin oxidation at 23° C in a sucrose formulation, %/year (From Ref - - l)... Fig. 9 The effect of residual water on the stability of freeze-dried proteins. Circles = human growth hormone deamidation and oxidation at 25° C, %/month squares = aggregation of human serum albumin at 50°C, %/day triangles = hemoglobin oxidation at 23° C in a sucrose formulation, %/year (From Ref - - l)...
Dialyser hypersensitivity syndrome (SEDA-11, 219) (SEDA-11, 479) presents as an acute anaphylactic reaction, the symptoms of which range from mild to hfe-threatening. The cause of the syndrome is unknown, but affected patients appear to have a high incidence of positive radioabsorbent tests to a conjugate of human serum albumin and ethylene oxide used to sterilize artificial kidneys. This conjugate may be the allergen responsible. [Pg.1298]

Immediate hypersensitivity reactions occurred in six of 600 donors who underwent automated platelet pheresis skin-prick testing in four of them (but in none of 40 controls) was positive when an ethylene oxide human serum albumin reagent was used (18). RadioaUergosorbent testing showed that serum from four of the six donors, but only one of 145 controls, contained IgE antibodies to ethylene oxide-albumin. [Pg.1298]

It seems worth pointing out, that 137 and human serum albumin contain no pendant phosphines and the donor atoms in the complexes formed with rhodium can be only O (137) or O, N and perhaps S (HSA), which are not the most suitable for stabilizing low oxidation state metal ions. Still these macroligands gave active and stable catalysts with rhodium, which shows that perhaps in the high local concentration provided by the polymer even these hard donor atoms are able to save the metal ion against hydrolysis or other deterioration. [Pg.175]

Digoxin human serum albumin conjugate (Dig-HSA) and ovalbumin conjugate (Dig-OVA) were prepared by a periodate oxidation method (21, 22) and used as an immunogen and a coating antigen, respectively. This method includes the following three steps and the proposed mechanism is shown in Fig. 4. [Pg.367]

Meucci E, Mordente A, Martorana G E (1991). Metal-catalyzed oxidation of human serum albumin Conformational and functional changes. J. Biol. Chem. 266 4692-4699. [Pg.407]

Modification of human serum albumin by o-glucose impaired its antiapoptotic activity for endothelial cells a 50% loss of activity corresponded to about four fiuctosamine residues per protein molecule. In another study, D-fiuctose-albumin enhanced nitric oxide synthase activity and a consequent NO-dependent apoptosis in vascular endothelial cells. " This effect was also attributed to a possible mechanism of hyperglycemia-induced vasculopathy in diabetic patients. In proximal tubular epithelial cells, however, the effect of co-incubated D-fiuctose-albumin was the... [Pg.356]


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See also in sourсe #XX -- [ Pg.27 ]




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