Abstract
Alditol:NADP oxidoreductase has been isolated and purified to homogeneity from human placenta. The enzyme has substrate specficities similar to those reported for partially purified alditol:NADP oxidoreductase from other mammalian species and has an approximate molecular weight of 39,000. The isolation of alditol:NADP oxidoreductase from human placenta supports the view that fructose synthesis from glucose in this tissue proceeds via the intermediate formation of sorbitol.
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