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Purification of dihydropteridine reductase from human platelets

✍ Scribed by Rong-Sen Shen; Dr. Creed W. Abell

Publisher: John Wiley and Sons
Year: 1981
Tongue: English
Weight: 490 KB
Volume: 6
Category: Article
ISSN: 0360-4012
DOI: 10.1002/jnr.490060205

No coin nor oath required. For personal study only.

✦ Synopsis

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Dihydropteridine reductase was purified approximately 1,700‐fold from human outdated blood platelets.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 K~m~ values for 2‐amino‐6,7,‐dimethyl‐4‐hydroxydihydropteridine (46 μml;M vs 49 μml;M), but the A form has a K~m~ for NADH that is two times higher than that of the B form (20 μml;M vs 9 μml;M).

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