Open AccessPurification and Properties of Rat‐Liver Thioredoxin
Author(s) -
Larson Göran,
Larsson Agne
Publication year - 1972
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1972.tb01747.x
Subject(s) - thioredoxin , deoxyribonucleotides , dithiothreitol , ribonucleotide reductase , sephadex , ribonucleotide , biochemistry , escherichia coli , chemistry , polyacrylamide gel electrophoresis , thioredoxin reductase , column chromatography , enzyme , polyacrylamide , microbiology and biotechnology , chromatography , biology , nucleotide , protein subunit , gene
Rat liver thioredoxin, which could be reduced nonenzymatically by dithiothreitol, was identified by its ability to function as hydrogen donor in the conversion of ribonucleotides to deoxyribonucleotides catalyzed by ribonucleotide reductase both from the same tissue and from Escherichia coli. The latter enzyme was used to detect the reduced form of the thioredoxin during its purification which involved treatment at pH 5, chromatography on Sephadex G‐50, heat treatment, and DEAE‐cellulose chromatography. The isolated material was approximately 50% pure as determined by polyacrylamide electrophoresis. Liver thioredoxin is a heat‐stable protein of low molecular weight.