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Selenomethionine is readily available as a dietary supplement. It has been suggested by nutritionists that selenomethionine, as an organic form of selenium, is easier for the human body to absorb than selenite, which is an inorganic form. [8] It was determined in a clinical trial that selenomethionine is absorbed 19% better than selenite. [8]
For example, selenomethionine and selenocysteine are selenium-containing amino acids present in the human body. Selenomethionine participates in the synthesis of selenoproteins . [ 2 ] The reduction potential and pKa (5.47) of selenocysteine are lower than those of cysteine , making some proteins have antioxidant activity. [ 3 ]
In the United States, selenium deficiency is not common. A federal survey of food consumption determined that for women and men over the age of 19, average consumption from foods and beverages was 89 and 125 μg/day, respectively. For women and men of all ages fewer than 3% consumed less than the EAR. [33]
Methaneselenol (commonly named "methylselenol") (CH 3 SeH), which can be produced in vitro by incubating selenomethionine with a bacterial methionine gamma-lyase (METase) enzyme, by biological methylation of selenide ion or in vivo by reduction of methaneseleninic acid (CH 3 −Se(=O)−OH), has been invoked to explain the anticancer activity ...
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Organoselenium compounds are required for cellular defense against oxidative damage and for the correct functioning of the immune system. They may also play a role in prevention of premature aging and cancer. The source of Se used in biosynthesis is selenophosphate. Glutathione oxidase is an enzyme with a selenol at its active site ...
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The thyroid gland and every cell that uses thyroid hormone also use selenium, [117] which is a cofactor for the three of the four known types of thyroid hormone deiodinases, which activate and then deactivate various thyroid hormones and their metabolites; the iodothyronine deiodinases are the subfamily of deiodinase enzymes that use selenium ...
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