Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

A multidisciplinary challenge to assess the next-generation risks of low-dose-rate long-term gamma-ray exposure by whole-genome sequencing in the mouse model.

Annals of the ICRP·2026
Same author

Data that revolutionise the fundamentals of radiation protection over 100 years and WAM model.

Annals of the ICRP·2026
Same author

Statistical analysis of low dose rate mouse experiments with WGS technology and quantitative reproduction of mutation frequency using the whack-a-mole model.

Annals of the ICRP·2026
Same author

Relationship between environmental radiation and radioactivity and childhood thyroid cancer found in Fukushima health management survey.

Scientific reports·2020
Same author

Advanced glycation end-products increase IL-6 and ICAM-1 expression via RAGE, MAPK and NF-κB pathways in human gingival fibroblasts.

Journal of periodontal research·2017
Same author

YKL-40 level in gingival crevicular fluid from patients with periodontitis and type 2 diabetes.

Oral diseases·2015

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.

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.

Related Experiment Videos

  • 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.