Quinonoid dihydropterin reductase from beef liver

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Abstract
Quinonoid dihydropterin reductase was purified from beef liver. This enzyme was indistinguishable from the reductase of sheep liver in MW, subunit composition, and terminal residues. Both beef and sheep liver reductases possessed acyl isoleucine as the N-terminal residue. Use of improved isolation techniques, including general ligand affinity chromatography, has yielded enzyme preparations of much higher specific activity than previously reported. Affinity chromatography experiments also suggested that the enzymic reaction proceeded by a compulsory ordered mechanism.