Purification of dihydropteridine reductase from human platelets

Dihydropteridine reductase was purified approximately 1,700‐fold from human outdated blood platelets.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 μml;M vs 49 μml;M), but the A form has a Km for NADH that is two...

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Veröffentlicht in:	Journal of neuroscience research 1981, Vol.6 (2), p.193-201
Hauptverfasser:	Shen, Rong-Sen, Abell, Creed W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Blood Platelets - enzymology Chromatography dihydropteridine reductase dihydropteridine reductase (NADH) Dihydropteridine Reductase - isolation & purification human Humans Kinetics man multiple forms NAD - analysis NADH, NADPH Oxidoreductases - isolation & purification platelets purification
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Zusammenfassung:	Dihydropteridine reductase was purified approximately 1,700‐fold from human outdated blood platelets.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 μml;M vs 49 μml;M), but the A form has a Km for NADH that is two times higher than that of the B form (20 μml;M vs 9 μml;M).
ISSN:	0360-4012 1097-4547
DOI:	10.1002/jnr.490060205