Isolation and characterization of aldose reductase and aldehyde reductase II from bovine lens

B. Das, G. A. Hair, Naseem Ansari, Satish Srivastava

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Aldose reductase (EC 1.1.1.21) and aldehyde reductase II (L-hexonate dehydrogenase, EC 1.1.1.2) from bovine lens were purified by a combination of DEAE-cellulose, polybuffer exchanger 94, NADP-affinity, and Sephadex G-100 gel filtration chromatographies. Both enzymes are monomers of Mr in the range of 32,000. Aldose reductase has a pI of 5.64 and the pH optimum at 6.2, whereas aldehyde reductase II demonstrate a pI of 6.45 and pH optimum at 7.0. While both the enzymes have wide overlapping substrate specificity and inhibition properties, aldose reductase specifically utilizes aldo-sugars as substrates and is more susceptible to inhibition by Sorbinil and tetramethylene glutaric acid as compared to aldehyde reductase II. Aldehyde reductase II is more susceptible to inhibition by phenobarbital as compared to aldose reductase. The two enzymes are immunologically distinct.

Original languageEnglish (US)
Pages (from-to)233-247
Number of pages15
JournalLens Research
Volume5
Issue number3-4
StatePublished - 1988

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L-glucuronate reductase
Aldehyde Reductase
Lenses
Enzymes
DEAE-Cellulose
Phenobarbital
Substrate Specificity
NADP
Gel Chromatography

ASJC Scopus subject areas

  • Ophthalmology

Cite this

Isolation and characterization of aldose reductase and aldehyde reductase II from bovine lens. / Das, B.; Hair, G. A.; Ansari, Naseem; Srivastava, Satish.

In: Lens Research, Vol. 5, No. 3-4, 1988, p. 233-247.

Research output: Contribution to journalArticle

Das, B. ; Hair, G. A. ; Ansari, Naseem ; Srivastava, Satish. / Isolation and characterization of aldose reductase and aldehyde reductase II from bovine lens. In: Lens Research. 1988 ; Vol. 5, No. 3-4. pp. 233-247.
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