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J Biol Chem, Vol. 273, Issue 44, 28708-28712, October 30, 1998
,
From the We have isolated a cDNA clone for a novel
glutathione-dependent dehydroascorbate reductase from a rat
liver cDNA library in Department of Biochemistry, Wakayama Medical
College, Wakayama 641-0012, Japan and the § Department of
Experimental Pathology, University of Pisa, I-56126 Pisa, Italy
gt11 by immunoscreening. The authenticity
of the clone was confirmed as follows: first, the antibody that had
been purified through affinity for the protein expressed by the cloned
gt11 phage recognized only the enzyme in a crude extract from rat
liver; and second, two internal amino acid sequences of purified enzyme
were identified in the protein sequence predicted from the cDNA.
The predicted protein consists of 213 amino acids with a molecular
weight of 24,929, which is smaller by ~3,000 than the value obtained
by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. This discrepancy of the molecular weight was explained by
post-translational modification because the recombinant protein expressed by a mammalian system (Chinese hamster ovary cells) was of
the same size as rat liver enzyme but larger than the protein expressed
by a bacterial system (Escherichia coli). Chinese hamster ovary cells, originally devoid of glutathione-dependent
dehydroascorbate reductase activity, was made to elicit the enzyme
activity (1.5 nmol/min/mg of cytosolic protein) by expression of the
recombinant protein. Additionally, the cells expressing the enzyme were
found to accumulate 1.7 times as much ascorbate as the parental cells after incubation with dehydroascorbate. This result points to the
importance of the dehydroascorbic acid reductase in maintaining a high
concentration of ascorbate in the cell.
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