A naphthoquinone adsorbent for affinity chromatography of human dihydropteridine reductase.

Abstract

1. A 1,2-naphthoquinone adsorbent is described which allows simple purification of dihydropteridine reductase directly from crude extract. 2. The native molecular weight indicates that a tetramer structure of the species is isolated by this method; this is unusual and possibly reflects the capacity of the procedure to preserve the native state of the enzyme.

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@article{Cotton1978ANA, title={A naphthoquinone adsorbent for affinity chromatography of human dihydropteridine reductase.}, author={Richard G. H. Cotton and Ian G. Jennings}, journal={European journal of biochemistry}, year={1978}, volume={83 1}, pages={319-24} }