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Related Experiment Videos

NADH-dependent dehydroascorbate reductase in the rabbit lens.

I Akatsuka1, M Bando, H Obazawa

  • 1Department of Ophthalmology, Tokai University Tokyo Hospital, Japan.

The Tokai Journal of Experimental and Clinical Medicine
|October 11, 2001
PubMed
Summary

Rabbit lens soluble fraction contains NADH-dependent dehydroascorbate (DHA) reductase activity. This enzyme, associated with beta-crystallin and lambda-crystallin, may enhance the lens's antioxidant capacity.

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Area of Science:

  • Biochemistry
  • Ophthalmology
  • Protein Chemistry

Background:

  • The lens's transparency and function rely on maintaining a reduced environment.
  • Antioxidant systems are crucial for protecting the lens from oxidative damage, particularly from UV light.

Purpose of the Study:

  • To identify and characterize NADH-dependent dehydroascorbate (DHA) reductase activity in the rabbit lens.
  • To investigate the protein components associated with this enzymatic activity.
  • To explore the potential role of this reductase in the lens's antioxidant defense mechanisms.

Main Methods:

  • Soluble fraction preparation from rabbit lens.
  • Enzyme assays for DHA reductase activity using NADH.
  • Gel filtration chromatography (Sephadex G-75) to assess molecular size.

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  • Ion-exchange chromatography (DEAE-cellulose) for protein separation.
  • SDS-PAGE to analyze protein subunit composition.

    • Main Results:

    • NADH-dependent DHA reductase activity was detected in the rabbit lens soluble fraction.
    • The enzyme exhibited specific kinetics with apparent Km values of 5.7 mM for DHA and 4.0 µM for NADH.
    • Activity co-eluted with oligomeric betaL1-crystallin and potentially lambda-crystallin fractions.
    • DEAE-cellulose chromatography revealed that ~80% of DHA reductase activity resided in fractions containing beta-crystallin and/or lambda-crystallin subunits.
    • SDS-PAGE identified common protein subunits of 32-33, 27, and 25 kDa in active fractions.

    Conclusions:

    • Oligomers of beta-crystallin and/or lambda-crystallin subunits are likely associated with NADH-dependent DHA reductase activity in the rabbit lens.
    • This reductase may play a significant role in enhancing the lens's antiphotoxidation capacity, contributing to ocular health.