Oxidation of L-ascorbic acid to dehydroascorbic acid on the surface of the red blood cell
Conference
·
· Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:7024369
L-ascorbic acid-1-/sup 14/C when incubated with human blood did not bind irreversibly to any of the protein components of plasma but did migrate irreversibly into erythrocytes. Isolation and characterization via IR of the moiety trapped within the cell established its identity as apparently, unchanged L-ascorbic acid. When dehydroascorbic acid-1-/sup 14/C was incubated with human blood, the results were identical including the identity of the entrapped moiety, L-ascorbic acid. It was found that L-ascorbic acid was enzymatically oxidized on the surface of the red blood cell to dehydroascorbic acid which diffused through the lipid soluble portion of the cell membrane and was enzymatically reduced back to ascorbic acid within the cell.
- Research Organization:
- Ball State Univ., Muncie, IN
- OSTI ID:
- 7024369
- Report Number(s):
- CONF-8606151-
- Conference Information:
- Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:6
- Country of Publication:
- United States
- Language:
- English
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