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Dehydroascorbate reductase activity in bovine lens

C Rose1, P S Devamanoharan, S D Varma

  • 1Department of Ophthalmology, University of Maryland School of Medicine, Baltimore 21201, USA.

International Journal for Vitamin and Nutrition Research. Internationale Zeitschrift Fur Vitamin- Und Ernahrungsforschung. Journal International De Vitaminologie Et De Nutrition
|January 1, 1995
PubMed
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Bovine lens mitochondria contain dehydroascorbate reductase, crucial for reducing dehydroascorbate to ascorbate. This enzymatic activity, vital during oxidative stress, utilizes glutathione as an electron donor.

Area of Science:

  • Biochemistry
  • Ophthalmology
  • Cell Biology

Background:

  • The bovine lens is susceptible to oxidative stress, impacting vision.
  • Ascorbate (Vitamin C) plays a critical antioxidant role in the lens.
  • Dehydroascorbate reductase activity is essential for maintaining ascorbate levels.

Purpose of the Study:

  • To investigate the presence and localization of dehydroascorbate reductase activity in the bovine lens.
  • To characterize the kinetic properties of this enzyme.
  • To understand the role of this enzyme in lens oxidative stress response.

Main Methods:

  • Isolation of mitochondrial and cytosolic fractions from bovine lens cortex-epithelium.
  • Assay of dehydroascorbate reductase activity in isolated fractions.

Related Experiment Videos

  • Determination of kinetic parameters, including Km for dehydroascorbate.

    • Main Results:

    • Dehydroascorbate reductase activity was primarily localized to the mitochondrial fraction.
    • No significant activity was detected in the cytosolic fraction.
    • The Michaelis constant (Km) for dehydroascorbate was determined to be approximately 0.45 mM.

    Conclusions:

    • Mitochondria possess enzymatic and non-enzymatic pathways for dehydroascorbate reduction to ascorbate, utilizing glutathione.
    • The enzymatic reduction may become more significant under oxidative stress conditions causing glutathione depletion.
    • Mitochondrial localization suggests a key role in managing oxidative conditions within the lens.