Dihydropteridine reductase, which catalyses the reduction of quinoid dihydropteridines in the presence of NADH or NADPH, has been purified approximately 800‐fold from rat liver tissue. The specificity of the purified dihydropteridine reductase with respect to quinoid dihydropteridine has been studied, by comparing the Michaelis constants and maximum velocity in systems containing the same concentration of enzyme. In addition, the inhibitory effect of some 2,4‐diaminopteridines has been studied. Furthermore the present work shows, that the quinone reductase activity observed with a previously used dihydropteridine reductase preparation is attributable to the presence of a quinone reductase in this preparation.
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K.E. Lind (1972) studied this question.
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