Literature DB >> 6778466

An electrophoretically cryptic alcohol dehydrogenase variant in Drosophila melanogaster. I. Activity ratios, thermostability, genetic localization and comparison with two other thermostable variants.

J B Gibson, G K Chambers, A V Wilks, J G Oakeshott.   

Abstract

The alcohol dehydrogenase (ADH) variant ADH-FCh.D. has a secondary alcohol/primary alcohol activity ratio characteristic of ADH-S although it has an electrophoretic mobility inseparable from ADH-F. ADH-FCh.D. is distinguished from these two common ADH variants by being much more thermostable. Genetic analysis suggests tht ADH-FCh.D. is specified by an allele at the Adh locus. Biochemical comparisons show that ADH-FCh.D. has the same electrophoretic mobility, activity ratio and thermostability as the two other heat-resistant variants which have been reported, ADH-F71K in Europe and ADH-Fr in North America. The geographically widespread distribution of a thermostable ADH variant within the ADH-F electrophoretic class indicates that it should be considered in attempts to explain the Adh polymorphism in natural populations.

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Year:  1980        PMID： 6778466     DOI： 10.1071/bi9800479

Source DB:  PubMed          Journal:  Aust J Biol Sci        ISSN： 0004-9417


  12 in total

1.  The partial characterization of alcohol dehydrogenase null alleles from natural populations of Drosophila melanogaster.

Authors:  A L Freeth; J B Gibson; H G de Couet
Journal:  Biochem Genet       Date:  1986-12       Impact factor: 1.890

2.  sn-Glycerol-3-phosphate oxidase and alcohol tolerance in Drosophila melanogaster larvae.

Authors:  S W McKechnie; B W Geer
Journal:  Biochem Genet       Date:  1986-12       Impact factor: 1.890

3.  The alcohol dehydrogenase alleloenzymes AdhS and AdhF from the fruitfly Drosophila melanogaster: an enzymatic rate assay to determine the active-site concentration.

Authors:  J O Winberg; R Hovik; J S McKinley-McKee
Journal:  Biochem Genet       Date:  1985-04       Impact factor: 1.890

4.  Effects of environmental temperatures on alcohol dehydrogenase activity levels in Drosophila melanogaster.

Authors:  B M Sampsell; V C Barnette
Journal:  Biochem Genet       Date:  1985-02       Impact factor: 1.890

5.  Variation in the biochemical properties of the Drosophila alcohol dehydrogenase allozymes.

Authors:  G K Chambers; A V Wilks; J B Gibson
Journal:  Biochem Genet       Date:  1984-02       Impact factor: 1.890

6.  Genetic variation at the alcohol dehydrogenase locus in Drosophila melanogaster: a third ubiquitous allele.

Authors:  J B Gibson; A V Wilks; G K Chambers
Journal:  Experientia       Date:  1982-06-15

7.  Structural analysis of an electrophoretically cryptic alcohol dehydrogenase variant from an Australian population of Drosophila melanogaster.

Authors:  G K Chambers; W G Laver; S Campbell; J B Gibson
Journal:  Proc Natl Acad Sci U S A       Date:  1981-05       Impact factor: 11.205

8.  Alcohol dehydrogenase thermostability variants in Drosophila melanogaster: comparison of activity ratios and enzyme levels.

Authors:  B Sampsell; E Steward
Journal:  Biochem Genet       Date:  1983-12       Impact factor: 1.890

9.  The purification and biochemical properties of alcohol dehydrogenase--"fast (Chateau Douglas)" from Drosophila melanogaster.

Authors:  G K Chambers
Journal:  Biochem Genet       Date:  1984-06       Impact factor: 1.890

10.  Drosophila melanogaster alcohol dehydrogenase. Biochemical properties of the NAD+-plus-acetone-induced isoenzyme conversion.

Authors:  J O Winberg; J S McKinley-McKee
Journal:  Biochem J       Date:  1988-04-01       Impact factor: 3.857
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