Ascorbate free radical reductase activity in vertebrate lenses of certain species

Shuji Matsukura, Masayasu Bando, Hajime Obazawa, Mikako Oka, Makoto Takehana

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Purpose: To clarify the function of ascorbate free radical (AFR) reductase in the antioxidation system of different vertebrate lenses. Methods: The soluble and insoluble fractions were prepared from bullfrog, guinea pig, rat, rabbit, swine, and bovine lenses, and membrane-bound enzymes in the insoluble fraction were extracted by 0.3% Triton X-100. Ascorbate free radical reductase and diaphorase activities in each fraction were determined. Results: Ascorbate free radical reductase activity in the lens soluble fraction was the highest in the bullfrog. That in the guinea pig and rabbit was at the next level. There was only a little activity in rat and swine lenses, and none was detected in the bovine lenses. However, a large species difference in AFR reductase activity was not observed in the 0.3% Triton X-100 extracts. Diaphorase activity was three to nine higher than AFR reductase activity in the soluble fractions of bullfrog, guinea pig, and rabbit. In the 0.3% Triton X-100 extracts of all animal species used, it was very high, 108 to 311 times the AFR reductase activity. Conclusion: These results indicate that the lens soluble and membrane-bound AFR reductase in the different animals may be individual enzyme molecules and have different antioxidative functions. Because the lenses of bullfrog, guinea pig, and rabbit are known to contain a near-ultraviolet (UV) light-absorbing compound, reduced pyridine nucleotide, at a high concentration, the soluble AFR reductase activity is expected to be high in the vertebrate lenses with a near-UV light filter, to enhance the antiphoto-oxidation capacity of ascorbate.

Original languageEnglish
Pages (from-to)233-239
Number of pages7
JournalJapanese Journal of Ophthalmology
Volume45
Issue number3
DOIs
Publication statusPublished - 2001 May

Fingerprint

Lenses
Vertebrates
Rana catesbeiana
Octoxynol
Guinea Pigs
Rabbits
Ultraviolet Rays
Swine
Membranes
free radical reductase
Enzymes
Nucleotides

Keywords

  • Antioxidation
  • Ascorbate free radical reductase
  • Lens membrane fraction
  • Lens soluble fraction
  • Near-UV light filter

ASJC Scopus subject areas

  • Ophthalmology

Cite this

Ascorbate free radical reductase activity in vertebrate lenses of certain species. / Matsukura, Shuji; Bando, Masayasu; Obazawa, Hajime; Oka, Mikako; Takehana, Makoto.

In: Japanese Journal of Ophthalmology, Vol. 45, No. 3, 05.2001, p. 233-239.

Research output: Contribution to journalArticle

Matsukura, Shuji ; Bando, Masayasu ; Obazawa, Hajime ; Oka, Mikako ; Takehana, Makoto. / Ascorbate free radical reductase activity in vertebrate lenses of certain species. In: Japanese Journal of Ophthalmology. 2001 ; Vol. 45, No. 3. pp. 233-239.
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abstract = "Purpose: To clarify the function of ascorbate free radical (AFR) reductase in the antioxidation system of different vertebrate lenses. Methods: The soluble and insoluble fractions were prepared from bullfrog, guinea pig, rat, rabbit, swine, and bovine lenses, and membrane-bound enzymes in the insoluble fraction were extracted by 0.3{\%} Triton X-100. Ascorbate free radical reductase and diaphorase activities in each fraction were determined. Results: Ascorbate free radical reductase activity in the lens soluble fraction was the highest in the bullfrog. That in the guinea pig and rabbit was at the next level. There was only a little activity in rat and swine lenses, and none was detected in the bovine lenses. However, a large species difference in AFR reductase activity was not observed in the 0.3{\%} Triton X-100 extracts. Diaphorase activity was three to nine higher than AFR reductase activity in the soluble fractions of bullfrog, guinea pig, and rabbit. In the 0.3{\%} Triton X-100 extracts of all animal species used, it was very high, 108 to 311 times the AFR reductase activity. Conclusion: These results indicate that the lens soluble and membrane-bound AFR reductase in the different animals may be individual enzyme molecules and have different antioxidative functions. Because the lenses of bullfrog, guinea pig, and rabbit are known to contain a near-ultraviolet (UV) light-absorbing compound, reduced pyridine nucleotide, at a high concentration, the soluble AFR reductase activity is expected to be high in the vertebrate lenses with a near-UV light filter, to enhance the antiphoto-oxidation capacity of ascorbate.",
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AB - Purpose: To clarify the function of ascorbate free radical (AFR) reductase in the antioxidation system of different vertebrate lenses. Methods: The soluble and insoluble fractions were prepared from bullfrog, guinea pig, rat, rabbit, swine, and bovine lenses, and membrane-bound enzymes in the insoluble fraction were extracted by 0.3% Triton X-100. Ascorbate free radical reductase and diaphorase activities in each fraction were determined. Results: Ascorbate free radical reductase activity in the lens soluble fraction was the highest in the bullfrog. That in the guinea pig and rabbit was at the next level. There was only a little activity in rat and swine lenses, and none was detected in the bovine lenses. However, a large species difference in AFR reductase activity was not observed in the 0.3% Triton X-100 extracts. Diaphorase activity was three to nine higher than AFR reductase activity in the soluble fractions of bullfrog, guinea pig, and rabbit. In the 0.3% Triton X-100 extracts of all animal species used, it was very high, 108 to 311 times the AFR reductase activity. Conclusion: These results indicate that the lens soluble and membrane-bound AFR reductase in the different animals may be individual enzyme molecules and have different antioxidative functions. Because the lenses of bullfrog, guinea pig, and rabbit are known to contain a near-ultraviolet (UV) light-absorbing compound, reduced pyridine nucleotide, at a high concentration, the soluble AFR reductase activity is expected to be high in the vertebrate lenses with a near-UV light filter, to enhance the antiphoto-oxidation capacity of ascorbate.

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