Heterogeneity of ascorbate free radical reductase in the human lens.

Masayasu Bando, Hajime Obazawa, Makoto Takehana

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The soluble ascorbate free radical (AFR) reductases in the human lens were separated into many isoforms in the range of pI 5-7 by native isoelectric focusing. In the two-dimensional gel electrophoresis, however, two main proteins with molecular weights of 20-25 kD were commonly identified to each isoform. The observed heterogeneity of the human lens AFR reductase is very similar to those reported for beta- and gamma-crystallins in aged and cataractous human lenses. From these results, it is suggested that some of the isoforms of the lens AFR reductase, especially the more acidic isoforms, may be formed by posttranslational modifications.

Original languageEnglish
Pages (from-to)143-149
Number of pages7
JournalDevelopments in Ophthalmology
Volume35
Publication statusPublished - 2002

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Lenses
Protein Isoforms
beta-Crystallins
gamma-Crystallins
Electrophoresis, Gel, Two-Dimensional
Isoelectric Focusing
Post Translational Protein Processing
Molecular Weight
free radical reductase
Proteins

Cite this

Heterogeneity of ascorbate free radical reductase in the human lens. / Bando, Masayasu; Obazawa, Hajime; Takehana, Makoto.

In: Developments in Ophthalmology, Vol. 35, 2002, p. 143-149.

Research output: Contribution to journalArticle

Bando, M, Obazawa, H & Takehana, M 2002, 'Heterogeneity of ascorbate free radical reductase in the human lens.', Developments in Ophthalmology, vol. 35, pp. 143-149.
Bando, Masayasu ; Obazawa, Hajime ; Takehana, Makoto. / Heterogeneity of ascorbate free radical reductase in the human lens. In: Developments in Ophthalmology. 2002 ; Vol. 35. pp. 143-149.
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