Abstract
Dihydropteridine reductase was purified approximately 1,700-fold from human outdated blood platelets. Two forms of the enzyme, A and B, were resolved. They have the same Km values for 2-amino-6,7,-dimethyl-4-hydroxydihydropteridine (46 microM vs 49 microM), but the A form has a Km for NADH that is two times higher than that of the B form (20 microM vs 9 microM).
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Blood Platelets / enzymology*
-
Chromatography
-
Dihydropteridine Reductase / isolation & purification*
-
Humans
-
Kinetics
-
NAD / analysis
-
NADH, NADPH Oxidoreductases / isolation & purification*
Substances
-
NAD
-
Dihydropteridine Reductase
-
NADH, NADPH Oxidoreductases