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Bovine 3-oxidation

Pepsin (pancreative, porcine and bovine Oxidation of methionine residues Loss of enzyme properties (K13)... [Pg.190]

Neely, M.D., Swift, L.L., and Montine, T.J. 2000. Human, but not bovine, oxidized cerebral spinal fluid lipoproteins disrupt neuronal rnicrombules. Lipids, 35(11), 1249. [Pg.170]

Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawaitoh K, Nakashima R, Yaono R and Yoshikawa S 1995 Structures of metai sites of oxidized bovine heart cytochrome c oxidase at 2.8 angstrom Science 269 1069-74... [Pg.2994]

A second method uses sodium periodate (NaI04) as the oxidant in the presence of the readily available protein bovine serum albumin. In this procedure, the sulfide is complexed in the chiral envirorunent of the protein. Although the oxidant is achiral, it encounters the sulfide in a chiral envirorunent in which the two faces of the sulfide are differentiated. [Pg.108]

Much higher asymmetric induction was observed in the two-phase oxidation of simple alkyl aryl and diaryl sulphides296, substituted alkyl aryl sulphides297 and dithioacetals of formaldehyde298 by sodium metaperiodate in the presence of proteins such as bovine serum y-globulin and egg albumin. Optical purities of the sulphoxides so formed ranged between 20 and 85%. [Pg.292]

Fig. 18. pH dependence of the oxidized Rieske fragment from bovine heart mitochondria (ISF). (a) Redox potential determined by cyclic voltammetry. The line was fitted to the data points, giving = 7.6 and pi a, x2 = 9-2. (b) CD intensity of the oxidized... [Pg.141]

Isab, A.A., Shaw, C.E. Ill and Locke, J. (1988) GC-MS and oxygen-17 NMR tracer studies of triethylphosphine oxide formation from auranofin and water- O in the presence of bovine serum albumin an in vitro model for auranofin metabolism. Inorganic Chemistry, 27, 3406-3409. [Pg.315]

The direct effect of both reduced and oxidized glutathione on the activity of an isolated bovine ventricular... [Pg.63]

Although it is widely accepted that ischaemia/ reperfusion-induced oxidant stress is associated with a reduction of Na/K ATPase activity, it is difficult to determine which features of this process are responsible for this effect. A classical approach to this type of problem has been to determine the effect of the application of selected metabolites or agents on the activity of the enzyme of interest, an approach that has been exploited for the sarcolemmal Na/K ATPase and glutathione (Haddock et al., 1990). The application of GSH (O.l-l.OmM) induces a concentration-dependent increase in the activity of a bovine isolated ventricular Na/K ATPase preparation (determined by the ouabain-sensitive hydrolysis of ATP to release inorganic phosphate). In the presence of 1 mM GSH there was a 38% stimulation of activity compared to untreated control... [Pg.64]

Figure 4.9 Effect of reduced glutathione (GSH) (0.25-1.0 ihm) and oxidized glutathione (GSSG) (0.25-1.0 mM) on ouabain-sensitive Na/K ATPase activity. An isolated Na/K ATPase preparation was prepared from fresh bovine ventricular tissue. Na/K ATPase activity was determined and quantified by the ouabain-sensitive hydrolysis of ATP to yield Inorganic phosphate. The rate of inorganic phosphate production was compared prior to and following the addition of either GSH or GSSG to the Incubation mixture. The data are presented as... Figure 4.9 Effect of reduced glutathione (GSH) (0.25-1.0 ihm) and oxidized glutathione (GSSG) (0.25-1.0 mM) on ouabain-sensitive Na/K ATPase activity. An isolated Na/K ATPase preparation was prepared from fresh bovine ventricular tissue. Na/K ATPase activity was determined and quantified by the ouabain-sensitive hydrolysis of ATP to yield Inorganic phosphate. The rate of inorganic phosphate production was compared prior to and following the addition of either GSH or GSSG to the Incubation mixture. The data are presented as...
Hydrogen peroxide is present in normal aqueous (approximately 30 /imol/1) whilst mean concentrations of around 70 tmol/l have been reported in aqueous from patients with cataracts, supporting a role for oxidative damage in the formation of cataracts (Spector and Garner, 1981). Diamine oxidase is one of the few enzymes to have been detected in bovine aqueous humour (albeit in trace quantities). It has been su ested that the hydrogen peroxide present in aqueous may be the product of the oxidative deamination of diamine substrates. This hypothesis is still unproven, since diamine oxidase substrates have not been identified in aqueous humour. [Pg.130]

Barker CD, Reda T, Hirst J. 2007. The flavoprotein suhcomplex of complex I (NADH ubiquinone oxidoreductase) from bovine heart mitochondria Insights into the mechanisms of NADH oxidation and NAD reduction from protein film voltammetry. Biochemistry 46 3454-3464. [Pg.630]

Salvemini, D., Korbut, R Anggard, E., and Vane, J., Immediate release of nitric oxide-like factor from bovine aortic endothelial cells by Escherichia coli lipopolysaccharide. Proc. Natl. Acad. Sci. USA. 87,2593-2597 (1990). [Pg.126]

Recent data indicate that SR-BI is a nonspecific receptor for many lipophilic molecules (Lorenzi et al., 2008 Reboul et al., 2007b). Apart from HDLs, rodent SR-BI also binds to LDL, VLDL, acetylated LDL, oxidized LDL, and maleylated bovine serum albumin. SR-BII has a similar ligand specificity and function to that of SR-BI (Webb et al., 1998). However, it has been shown that vitamin E (which like carotenoids is carried in the bloodstream mainly by LDL and HDL) is transported more efficiently into the endothelial cells from HDLs than from LDLs (Balazs et al., 2004 Kaempf-Rotzoll et al., 2003 Mardones and Rigotti, 2004). This is in striking contrast to cholesterol, which is taken up much more efficiently from LDLs than HDLs by the RPE to the retina (Tserentsoodol et al., 2006b). It remains to be shown which lipoproteins are the main carriers for carotenoids transported from blood into the RPE. [Pg.315]

Immobilized dihydrolipoamide (thioctic acid) (Gorecki and Patchornick, 1973 Gorecki and Patchornick, 1975) and immobilized N-acetyl-homocysteine thiolactone (Eldjarn and Jellum, 1963 Jellum, 1964) are the two most commonly used immobilized disulfide reductants. In addition, immobilized TCEP provides a reducing matrix that is free of thiols (Thermo Fisher). Such immobilized reductants successfully can be used to reduce many types of biological disulfides, including small molecules like oxidized glutathione and bovine insulin. They... [Pg.97]


See other pages where Bovine 3-oxidation is mentioned: [Pg.161]    [Pg.501]    [Pg.239]    [Pg.339]    [Pg.430]    [Pg.161]    [Pg.75]    [Pg.295]    [Pg.828]    [Pg.861]    [Pg.70]    [Pg.148]    [Pg.11]    [Pg.116]    [Pg.120]    [Pg.122]    [Pg.142]    [Pg.75]    [Pg.295]    [Pg.828]    [Pg.861]    [Pg.707]    [Pg.330]    [Pg.327]    [Pg.186]    [Pg.157]    [Pg.203]    [Pg.126]    [Pg.188]    [Pg.502]    [Pg.6]    [Pg.242]    [Pg.67]    [Pg.1026]   
See also in sourсe #XX -- [ Pg.21 ]




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