An efficient regeneration of vitamin C (ascorbate) from its oxidized byproduct, dehydroascorbate (DHAA), is necessary to maintain sufficient tissue levels of the reduced form of the vitamin. Additionally the recycling may be more significant in mammals, such as guinea pigs and humans, who have lost the ability to synthesize ascorbate de novo than it is in most other mammals who have retained the ability to synthesize the vitamin from glucose. Both a chemical and an enzymatic reduction of DHAA to ascorbate have been proposed. Several reports have appeared in which proteins, including thioltransferase, protein disulfide isomerase, and 3-α-hydroxysteroid dehydrogenase, characterized for other activities have been identified as having DHAA reductase activity in vitro. Whether these previously characterized proteins catalyze the reduction of DHAA in vivo is unclear. In the present study, a 66 kD protein was purified strictly on the basis of its DHAA-reductase activity and was identified as rat serum albumin. The protein was further characterized and results support the suggestion that serum albumin acts as an antioxidant and exerts a significant glutathione-dependent DHAA-reductase activity that may be important in the physiologic recycling of ascorbic acid.
|Original language||English (US)|
|Number of pages||8|
|Journal||Free Radical Biology and Medicine|
|State||Published - Jun 1999|
Bibliographical noteFunding Information:
This work was supported by National Institutes of Health Grant DK47953. We thank Willis K. Samson, Tonya Murphy, Melissa Benson, and Tim Meyer for all the laboratory assistance. We are also thankful to Steve Latshaw, Department of Biological Chemistry, the Chicago Medical School for sequencing the purified proteins.
- Ascorbic acid
- Free radicals
- Oxidative stress
- Protein purification
- Redox cycle