Purification of dihydropteridine reductase from human platelets

J Neurosci Res. 1981;6(2):193-201. doi: 10.1002/jnr.490060205.

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Dihydropteridine reductase was purified approximately 1,700-fold from human outdated blood platelets.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