Warning: The NCBI web site requires JavaScript to function. more...
Generate a file for use with external citation management software.
Department of Medicinal Biochemistry, Wellcome Research Laboratories, Research Triangle Park, North Carolina 27709.
The ability of the enzyme dihydrofolate reductase to catalyze the formation of tetrahydrobiopterin from dihydrobiopterin was used to develop a method for measuring the activity of this enzyme in vivo. This method can be used to determine the activity of the enzyme in tissues as well as the extent and duration of inhibition of the enzyme by antifolates. Sepiapterin, which is converted to dihydrobiopterin by the enzyme sepiapterin reductase, was as effective a precursor as dihydrobiopterin and has been used in these studies because of its greater stability relative to dihydrobiopterin. Assay conditions must be established for each tissue and enzyme activity can be determined either by measuring the rate of disappearance of dihydrobiopterin or the rate of formation of tetrahydrobiopterin.
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on