Purification and characterization of sepiapterin reductase from rat erythrocytes.

Abstract

Sepiapterin reductase from rat erythrocyte hemolysate was purified 2000-fold to apparent homogeneity with 30% yield. The specific activity of the purified enzyme was 18 units/mg protein, and its molecular weight was 55 000. The enzyme consists of two identical subunits, each of which has a molecular weight of 27 500. The enzyme showed a single peak by… (More)

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@article{Sueoka1982PurificationAC, title={Purification and characterization of sepiapterin reductase from rat erythrocytes.}, author={T Sueoka and Shigeki Katoh}, journal={Biochimica et biophysica acta}, year={1982}, volume={717 2}, pages={265-71} }