Enzymatic Synthesis of Deoxyribonucleotides. Iv. Isolation and Characterization of Thioredoxin, the Hydrogen Donor from Escherichia Coli B.

@article{Laurent1964EnzymaticSO,
  title={Enzymatic Synthesis of Deoxyribonucleotides. Iv. Isolation and Characterization of Thioredoxin, the Hydrogen Donor from Escherichia Coli B.},
  author={Torvard C. Laurent and Evan C Moore and Peter A Reichard},
  journal={The Journal of biological chemistry},
  year={1964},
  volume={239},
  pages={3436-44}
}
The reductive formation of deoxycytidine diphosphate from cytidine diphosphate with crude extracts of Escherichia coli B required the presence of reduced triphosphopyridine nucleotide (1). On purification of the GDP-reductase system, an enzyme fraction (Fraction B) was obtained, which was no longer active with TPNH but, instead, showed an absolute requirement for reduced lipoate (2, 3). Several lines of evidence suggested, however, that reduced lipoate acted as a model substance in the purified… CONTINUE READING