Rat lens aldehyde reductase

S. Sato, P. F. Kador

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Aldehyde reductase (E.C. has been purified to apparent homogeneity from rat lens and its properties have been compared to those of both rat lens aldose reductase and rat kidney aldehyde reductase. The purification was accomplished by ammonium sulfate fractionation, Sephadex G-75 chromatography, affinity chromatography on Amicon Gel Orange A and chromatofocusing. The purified enzyme is distinct from rat lens aldose reductase but appears similar to rat kidney aldehyde reductase in molecular weight, immunological properties and substrate specificities. Rat lens aldehyde reductase is inhibited by a number of aldose reductase inhibitors; however, its susceptibility to inhibition is more similar to rat kidney aldehyde reductase than to rat lens aldose reductase.

Original languageEnglish (US)
Pages (from-to)1618-1622
Number of pages5
JournalInvestigative Ophthalmology and Visual Science
Issue number7
StatePublished - 1989
Externally publishedYes

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience


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