PubMed · 3758216
Ascorbate regeneration in bovine ocular tissues by NADH-dependent semidehydroascorbate reductase.
Abstract
Despite its fast autoxidation in vitro, ascorbate remains in its reduced form in vivo, indicating a special mechanism may be involved in its regeneration. The presence of an NADH-dependent reductase system, semidehydroascorbate reductase (SDR), for regeneration of ascorbate from its partially oxidized form, semidehydroascorbate (SDA), was demonstrated in bovine ocular tissues after extraction in Triton X-100. Highest SDR activity was detected in retinal extracts in the order of retina greater than pigment epithelium-choroid = ciliary body greater than iris. Minimal or no activity was observed in lens extracts or in aqueous fluid. Freezing and thawing, or boiling, destroyed the NADH-dependent SDR activity. NADH oxidation was significantly reduced (22% of total activity) when assays with retinal extracts were performed at 5 degrees C. Treatment with 4 mM, N-ethylmaleimide reduced the rate of NADH oxidation to 73 or 42% compared with control values with retinal or ciliary body extracts, respectively.
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M Khatami, L E Roel, W Li, J H Rockey. 1986. Ascorbate regeneration in bovine ocular tissues by NADH-dependent semidehydroascorbate reductase.. https://doi.org/10.1016/s0014-4835(86)80084-7
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