𝔖 Bobbio Scriptorium
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In vivo measurement of dihydrofolate reductase and its inhibition by antifolates

✍ Scribed by Seaton W. Bowers; David S. Duch

Publisher
Elsevier Science
Year
1988
Tongue
English
Weight
545 KB
Volume
172
Category
Article
ISSN
0003-2697

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✦ Synopsis

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 ofthis enzyme in viva. 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.

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