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A Thioredoxin Induced by Bacteriophage T4

II. PURIFICATION AND CHARACTERIZATION

From the ¹ From the Department of Chemistry II, Karolinska Institutet, Stockholm, Sweden

T4 thioredoxin was purified from an extract of Escherichia coli B infected from T4 am 122. The protein was obtained in essentially pure form as judged from ultracentrifugation data, gel electrophoresis, and from the stoichiometry of its reaction with NADPH. The molecular weight was 10,400 as measured by sedimentation equilibrium centrifugation. This compares with a molecular weight of 11,700 for the host Escherichia coli thioredoxin. Amino acid analyses showed the presence of 88 to 89 amino acid residues including all common amino acids except tryptophan. The composition differs markedly from that of E. coli thioredoxin. In its oxidized form, T4 thioredoxin contains a single disulfide bridge which is reduced by NADPH in the presence of E. coli thioredoxin reductase. The oxidation-reduction potential of the couple T4 thioredoxin-S₂/T4 thioredoxin-(SH)₂ was -0.23 volt (pH 7.0, 20°), which is a significantly higher value than that of E. coli thioredoxin (-0.26 volt). Two phage mutants which failed to induce T4 thioredoxin activity were isolated.

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