Purification of Thioredoxin Reductase from the Novikoff Rat Tumor

Chin-Chun Chen Department of Biochemistry, The University of Texas System Cancer Center M. D. Anderson Hospital and Tumor Institute, Houston, Texas, 77030

Barbara L. Borns McCall Department of Biochemistry, The University of Texas System Cancer Center M. D. Anderson Hospital and Tumor Institute, Houston, Texas, 77030

E. Colleen Moore Department of Biochemistry, The University of Texas System Cancer Center M. D. Anderson Hospital and Tumor Institute, Houston, Texas, 77030

Abstract

Thioredoxin reductase (E. C. 1.6.4.5.) has been purified to about 95% homogeneity from the Novikoff ascites rat tumor. The enzyme contained two subunits of approximately 58, 000 daltons, with one FAD per subunit. The amino acid analysis is reported. An immunoadsorbent was prepared and used for affinity chromatography in order to improve the yield of the enzyme.

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Purification of Thioredoxin Reductase from the Novikoff Rat Tumor

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Purification of Thioredoxin Reductase from the Novikoff Rat Tumor

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