PMID: 3758216Aug 1, 1986Paper

Ascorbate regeneration in bovine ocular tissues by NADH-dependent semidehydroascorbate reductase

Experimental Eye Research
M KhatamiJ H Rockey

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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Citations

Jan 1, 1991·Comparative Biochemistry and Physiology. A, Comparative Physiology·R C Rose, A M Bode
Oct 1, 1994·Free Radical Biology & Medicine·B S WinklerT S Rex
Dec 1, 1987·Photochemistry and Photobiology·U P Andley
Oct 1, 1986·Experimental Eye Research·M KhatamiJ H Rockey
Jun 22, 1999·Experimental Eye Research·S A Keys, W F Zimmerman
Feb 3, 1998·Biochemical and Biophysical Research Communications·N WadaK Asada
Jul 1, 1993·Current Eye Research·A M BodeR C Rose
Mar 4, 1991·Biochimica Et Biophysica Acta·F J AlcainP Navas

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