1,721,004 research outputs found
ULTRA PERFORMANCE LIQUID CHROMATOGRAPHY AND FLUORESCENCE DETECTION FOR SIMULTANEOUS DETERMINATION OF ASYMMETRIC DIMETHYLARGININE, MONOMETHYLARGININE, SYMMETRIC DIMETTHYLARGININE AND L-ARGININE IN HUMAN PLASMA IN BIOLOGICAL FLUIDS
No full textVitamin A, beta carotene, licopene and vitamin E levels in human preovulatory follicular fluid
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Relationship between asymmetric dimethylarginine and asymptomatic carotid atherosclerosis.
No full textCompliance therapy with anti-inflammatory antiasthmatic drugs: inhaled corticosteroids and leukotryene receptor antagonists.
No full textVitamin A decreases after a maximal incremental stress test in non-professional male runners with low aerobic performance
No full textThe data on the effects of aerobic training on plasma antioxidant vitamins are conflicting. Additionally, most studies focus on the oxidative profiles of professional athletes, but limited information is available for amateur athlete populations. The aim of this study was to evaluate the effects of high-intensity exercise on antioxidant vitamins in non-professional runners with varying levels of aerobic power. Eighty-one male runners underwent an incremental test to exhaustion. The study population was then divided into the following tertiles according to VO,max: Group L (LOWVO2Max, 49.7). Comparative analyses were performed between Groups L and H. The total antioxidant capacity- (TAC), Vitamin (Yit) E, Vitamin A, p-carotene, lvcopene and thiobarbituric acid-reactive substances (TBARS) were determined before and 60 inin after exercise testing. After the stress test, Vit A decreased and TBARS increased in Group L, whereas no changes in the vitamin concentrations, TAC induction and TBARS reduction were observed in group H. In individuals with low VO,max, an incremental test determined lipid-peroxidation and Vitamin A consumption, whereas H Group increases TAC that buffer TBARS production
Blunted nocturnal fall in blood pressure and oxidative stress in men and women with essential hypertension.
No full textStructural and functional properties of the 34kDa fragment produced by the N-terminal chymotriptic cleavage of GSTP1-1
No full text-Limited proteolysis of glutathione transferase P1-1 (GSTP1-1) by chymotrypsin generates a 34-kDa GSTP1-1 fragment (a dimer of the 17-kDa subunit composed by residues 48-207) containing the whole C-terminal domain and a part (about 15%) of the N-terminal domain (residues 48-76, i.e., the structural elements beta 3, beta 4, and alpha C). The structural and functional properties of this large fragment have been investigated by analyzing its binding properties to 2-p-toluidinylnaphthalene-6-sulfonate (TNS) extrinsic probe, the TNS displacement technique, and the molecular modeling approach. The results obtained indicated that the 34-kDa GSTP1-1 fragment maintains an hydrophobic pocket with the same structural properties of the corresponding GSTP1-1 hydrophobic binding site. In addition, the 34-kDa GSTP1-1 binds a number of hydrophobic compounds such as 1-chloro-2,4-dinitrobenzene, hemin, and bilirubin with the same affinity of the native enzyme. Being structurally and functionally autonomous, this fragment, mostly constituted by domain II, appears as an independent folding unit in the protein. Nevertheless, in the entire native protein, interdomain interactions occur and are responsible for the major solvent exposure of the H-site in the presence of glutathion
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