The degradation of 6-selenoguanosine (NSC 137679) (I) in water and in various buffer systems was investigated. Drug degradation in aqueous media was monitored by high-pressure of I in various chromatography. Some kinetic aspects of the degradation of I in various buffer systems at 25 degrees also were studied spectrophotometrically. The degradation, which requires oxygen, involves autoxidation of I to the corresponding diselenide, which produces a selenide and metallic selenium in the presence of oxygen. This degradation pathway differs from that reported fro the oxidation of related thio compounds.
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The characterization of human selenocysteine lyase, an enzyme that specifically catalyzes the decomposition of L-selenocysteine to L-alanine and hydrogen selenide, is described. The enzyme is the first described that acts exclusively on a selenium compound. The enzyme from human tissues, analogous to that from pig tissues and bacteria, requires pyridoxal 5-phosphate as a cofactor.
View Article and Find Full Text PDFThe degradation of 6-selenoguanosine (NSC 137679) (I) in water and in various buffer systems was investigated. Drug degradation in aqueous media was monitored by high-pressure of I in various chromatography. Some kinetic aspects of the degradation of I in various buffer systems at 25 degrees also were studied spectrophotometrically.
View Article and Find Full Text PDF6-Selenoguanosine (NSC 137679) was stablized and formulated as a lyophilized parenteral paroduct using ascorbic acid as an antioxidant. In addition to preventing the oxidation of 6-selenoguanosine to the corresponding diselenide in aqueous solution, ascorbic acid reduced the diselenide already in the bulk drug. Dithioerythritol and sodium bisulfite also were evaluated as antioxidants.
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