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Cloning and sequencing of a human thioredoxin reductase
P Y Gasdaska1, J R Gasdaska, S Cochran
1Arizona Cancer Center, Tucson 85724, USA.
FEBS Letters
|October 2, 1995
Abstract:
The DNA sequence encoding human placental thioredoxin reductase has been determined. Of the 3826 base pairs sequenced, 1650 base pairs were in an open reading frame encoding a mature protein with 495 amino acids and a calculated molecular mass of 54,171. Sequence analysis showed strong similarity to glutathione reductases and other NADPH-dependent reductases. Human thioredoxin reductase contains the redox-active cysteines in the putative FAD binding domain and has a dimer interface domain not previously seen with prokaryote and lower eukaryote thioredoxin reductases.