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Titlebook: Selenium in Biology and Medicine; Proceedings of the 4 Albrecht Wendel Conference proceedings 1989 Springer-Verlag Berlin Heidelberg 1989 b

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Involvement of a Selenoprotein in Glycine, Sarcosine, and Betaine Reduction by , . (Dürre and Andreesen 1982, 1983), . (Dürre et al. 1983), and . (Lebertz and Andreesen 1988). Betaine reduction has so far only been studied with . (Naumann et al. 1983). The observed formation of trimethylamine was dependent on the presence of 1 µM selenite.
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Dependence of Mouse Liver Phospholipid Hydroperoxide Glutathione Peroxidase on Dietary Seleniumity released the free fatty acid hydroperoxides (Grossmann and Wendel 1983), the PHGPx acts directly upon complex lipid hydroperoxides even in the heterogeneous phase, i.e., in the form of micelles (Ursini and Bindoli 1987). On the other hand, the enzymatic rate of PHGPx towards H.O. is poor compared to GSH-Px.
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Active Oxygen Generation by the Reaction of Selenite with Reduced Glutathione in Vitro vitro hemolysis. In order to estimate the relationship between GSH and the selenite-induced lipid peroxidation, we have examined the active oxygen generation in the mixture of selenite and GSH by using luminol- or lucigenin-dependent chemiluminescence (CL) as an indicator.
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Conference proceedings 1989rite trace element, selenium. This meeting continued the good tradition of three previous meetings held in Corvallis/Oregon, 1976, in Lubbock/Texas, 1980, and in Beijing/China, in 1984. Incidentally, the University of Tiibingen provided a unique historical background for a Symposium devoted to recen
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The Regulation of Glutathione Peroxidase Gene Expression; Implication for Species Difference and theidative damage. GSH-Px protein contains a selenocysteine (Se-Cys) moiety in its active site, but the mechanism of Se-Cys incorporation into the polypeptide chain of the enzyme protein has long been unresolved. Chambers et al. (1986) discovered that a UGA termiation codon in the open reading frame of
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Regulation of Expression of Glutathione Peroxidase by Seleniumvery of an enzyme, glutathione peroxidase (GSH-Px, GSH: H.O. oxidoreductase, EC 1.11.1.9), that was important for protection of erythrocytes against hemolysis. These two discoveries, plus the apparent interaction of sulfur compounds with Se and GSH-Px, led J. T. Rotruck and W. G. Hoekstra at Wiscons
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Studies on New Selenoproteins and Specific Selenium Target Tissues skeletal muscle and the heart muscle, research has naturally concentrated on the role of Se in the affected tissues. Since the element was then identified as the essential component of glutathione peroxidase, the effects of Se have been investigated mainly with regard to the functions of this enzym
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Selenium-Containing Proteins in Plasma of Higher Primatese selenium peak eluted slightly ahead of the glutathione peroxidase (GPX) activity peak, suggesting that the majority of the plasma selenium may not be associated with GPX. In subsequent work (Beilstein and Whanger 1988), less than 10% of the selenium in plasma was calculated to be associated with G
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Involvement of a Selenoprotein in Glycine, Sarcosine, and Betaine Reduction by ,equires the presence of 1 µM selenite (optimum) as does the reduction of betaine, sarcosine, or creatine to acetate, methylamines and urea (Fig. 1) irrespective of NAD(P)H, H., formate, or e.g., valine being the reductant. However, growth on serine is independent of selenite addition as that on alan
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