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Journal article
Ascorbate regeneration in bovine ocular tissues by NADH-dependent semidehydroascorbate reductase
Experimental eye research, v 43(2), pp 167-175
1986
PMID: 3758216
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Abstract
Despite its fast autoxidation in vitro, ascorbate remains in its reduced from 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 > pigment epithelium-choroid = ciliary body > 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°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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Details
- Title
- Ascorbate regeneration in bovine ocular tissues by NADH-dependent semidehydroascorbate reductase
- Creators
- Mahin Khatami - Penn Presbyterian Medical CenterLawrence E. Roel - Penn Presbyterian Medical CenterWeiye Li - Penn Presbyterian Medical CenterJohn H. Rockey - Penn Presbyterian Medical Center
- Publication Details
- Experimental eye research, v 43(2), pp 167-175
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Ophthalmology [Historical]
- Web of Science ID
- WOS:A1986D969200004
- Scopus ID
- 2-s2.0-0022492130
- Other Identifier
- 991019298816204721
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Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Ophthalmology