Literature DB >> 469473

Aldehyde dehydrogenase of the Mongolian gerbil, Meriones unguiculatus.

F Simpson, R Lindhal.   

Abstract

The aldehyde dehydrogenase (Aldehyde:NAD(P) oxidoreductase E.C. 1.2.1.3. and 1.2.1.5) phenotype in several tissues of the Mongolian gerbil, Meriones unguiculatus, has been established. The tissue distribution of gerbil aldehyde dehydrogenase is similar to that of the rat, with liver possessing the majority of the aldehyde dehydrognease activity. Male kidney and testis possess significantly more activity than female kidney and ovary. The substrate and co-enzyme specificity of gerbil liver aldehyde dehydrogenase is also similar to that of rat and mouse liver. Gel isoelectric focusing resolves one major gerbil liver aldehyde dehydrogenase isozyme at pI 5.3. Mouse liver is resolved into two major isozymes at pIs 5.3 and 5.6 and rat liver aldehyde dehydrogenase into one major isozyme at pI 5.4. Gerbil liver aldehyde dehydrogenase is functional over a broad pH range with an optima at pH 9.0. Rat and mouse liver aldehyde dehydrogenase possess sharp pH optima at pH 8.5.

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Year:  1979        PMID: 469473     DOI: 10.1002/jez.1402070306

Source DB:  PubMed          Journal:  J Exp Zool        ISSN: 0022-104X


  2 in total

1.  Subcellular distribution and properties of aldehyde dehydrogenase from 2-acetylaminofluorene-induced rat hepatomas.

Authors:  R Lindahl
Journal:  Biochem J       Date:  1979-10-01       Impact factor: 3.857

2.  Bovine lens aldehyde dehydrogenase. Purification and preliminary characterization.

Authors:  H H Ting; M J Crabbe
Journal:  Biochem J       Date:  1983-11-01       Impact factor: 3.857

  2 in total

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