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J. Biol. Chem., Vol. 264, Issue 25, 14775-14777, Sep, 1989

Cloning and sequence determination of human placental aldose reductase gene

S Chung and J LaMendola
Department of Biological Chemistry, University of Illinois, Chicago 60612.

The human aldose reductase gene has been cloned by screening a human placental cDNA library with antibodies against bovine lens aldose reductase. The nucleotide sequence of the entire coding region has been determined. The deduced amino acid sequence indicates that the human enzyme is 84% identical to the bovine lens aldose reductase and 85% identical to the rat lens aldose reductase. It is also very similar to the human aldehyde reductase, the bovine prostaglandin F synthase, and to the European common frog rho-crystallin. The deduced amino acid sequence also indicates that maturation of aldose reductase involves removal of the N-terminal methionine.
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