Purification of thioredoxin reductase from the Novikoff rat tumor.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D006528:Carcinoma, Hepatocellular / Q000201:enzymology*; D005260:Female; D007163:Immunosorbent Techniques; D008113:Liver Neoplasms / Q000201:enzymology*; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification*; D009374:Neoplasms, Experimental / Q000201:enzymology; D051381:Rats; D013880:Thioredoxin-Disulfide Reductase / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*
D000596:Amino Acids; D009247:NADH, NADPH Oxidoreductases; D013880:Thioredoxin-Disulfide Reductase