Sepiapterin reductase in human amniotic and skin fibroblasts, chorionic villi, and various blood fractions
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Cited by (24)
Sepiapterin reductase mediates chemical redox cycling in lung epithelial cells
2013, Journal of Biological ChemistryCitation Excerpt :To confirm that sepiapterin reductase possesses redox cycling activity, the human and mouse genes were cloned into a hexahistidine-tagged vector, expressed in E. coli, and purified by nickel affinity chromatography (Fig. 2, panel D, inset, and data not shown). The enzymes, which appeared as single bands on SDS-polyacrylamide gels (Mr ≈30,000), reduced sepiapterin to BH2, as measured by decreases in absorption of sepiapterin at 420 nm (25) and by the formation of BH2 by HPLC (26). Similar enzyme activity was detected in both assays (Figs. 2, panel D, and 3, panels A and B, and data not shown).
Nuclear localization of tetrahydrobiopterin biosynthetic enzymes
2004, Biochimica et Biophysica Acta - General SubjectsLocalization of sepiapterin reductase in the human brain
2002, Brain ResearchCitation Excerpt :The enzyme activities were measured by using 10 μg of the brain homogenate, which was prepared as described above. SPR activity was assayed as described previously with a slight modification [11]. The incubation mixture (total volume of 50 μl) contained 100 mM potassium phosphate buffer (pH 6.4), 0.1 mM NADPH, and 0.15 mM sepiapterin as substrate.
Enhanced expression of GTP cyclohydrolase I in V-1-overexpressing PC12D cells
2002, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Measurement of SPR activity. SPR activity was assayed as described previously with a slight modification [13]. The incubation mixture (total volume of 50 μl) contained 100 mM potassium phosphate buffer (pH 6.4), 0.1 mM NADPH, and 0.15 mM sepiapterin as substrate.
Mutations in the sepiapterin reductase gene cause a novel tetrahydrobiopterin-dependent monoamine-neurotransmitter deficiency without hyperphenylalaninemia
2001, American Journal of Human GeneticsCitation Excerpt :For fibroblast cultures, the appropriate informed consent was obtained from all subjects. SR activity in red blood cells was assayed according to the method described by Ferre and Naylor (1988), with sepiapterin as a substrate and under assay conditions essentially the same as those for the fibroblasts (see the preceding paragraph). The assay monitors the conversion of sepiapterin to dihydrobiopterin, which is then measured as the oxidized product, biopterin.