PMID: 6410397Aug 1, 1983Paper

Biochemical and molecular analysis of naturally occurring Adh variants in Drosophila melanogaster

Proceedings of the National Academy of Sciences of the United States of America
S M Anderson, J F McDonald

Abstract

The results of a detailed analysis of the biochemical and molecular basis of alcohol dehydrogenase (ADH) activity variation existing among six naturally occurring and one ethyl methanesulfonate-induced Adh variant strain of Drosophila melanogaster are presented. Significant specific activity differences exist among the strains but the majority of ADH activity variation can be accounted for by differences in levels of ADH protein. These protein level differences can, in turn, be accounted for by ADH synthesis rate variation, which positively correlates with in vivo levels of cytoplasmic Adh mRNA. The functional variability is correlated with known structural variation in and around the area of the Adh gene.

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Citations

Jun 1, 1985·Biochemical Genetics·M A Johns, J H Postlethwait
Oct 1, 1987·Biochemical Genetics·J AlberolaA Fontdevila
Dec 1, 1988·Journal of Molecular Evolution·P W HeinstraG E Thorig
Jan 1, 1985·Comparative Biochemistry and Physiology. C, Comparative Pharmacology and Toxicology·R Gonzàlez-Duarte, L Vilageliu
Jul 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·C C Laurie, L F Stam
Dec 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·D L Crawford, D A Powers
Jun 15, 2015·Trends in Genetics : TIG·Jeffrey R AdrionBrandon S Cooper
Jun 4, 2019·Proceedings of the National Academy of Sciences of the United States of America·David W LoehlinSean B Carroll
May 29, 2007·PLoS Computational Biology·Scott W Doniger, Justin C Fay
Feb 1, 1999·Evolution; International Journal of Organic Evolution·Mauro SantosAntonio Fontdevila
Sep 21, 2006·The Journal of Experimental Biology·Kristi L MontoothAndrew G Clark

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