Purification and characterization of aldose reductase and aldehyde reductase from human kidney

N. H. Ansari, A. Bhatnagar, S. Liu, S. K. Srivastava

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

Aldose reductase and aldehyde reductases have been purified to homogeneity from human kidney and have molecular weights of 32,000 and 40,000 and isoelectric pH 5.8 and 5.3, respectively. Aldose reductase, beside catalyzing the reduction of various aldehydes, reduces aldo-sugars, whereas aldehyde reductase, does not reduce aldo-sugars. Aldose reductase activity is expressed with either NADH or NADPH as cofactor, whereas aldehyde reductase utilizes only NADPH. Both enzymes are inhibited to varying degrees by aldose reductase inhibitors. Antibodies against bovine lens aldose reductase precipitated aldose reductase but not aldehyde reductase. The sequence of addition of the substrates to aldehyde reductase is ordered and to aldose reductase is random, whereas for both the enzymes the release of product is ordered with NADP released last.

Original languageEnglish (US)
Pages (from-to)755-765
Number of pages11
JournalBiochemistry International
Volume25
Issue number4
StatePublished - 1991

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Purification and characterization of aldose reductase and aldehyde reductase from human kidney'. Together they form a unique fingerprint.

Cite this