Participation of Drosophila melanogaster alcohol dehydrogenase (ADH) in the detoxification of 1-pentene-3-ol and 1-pentene-3-one
Author:
Publisher
Springer Science and Business Media LLC
Subject
Genetics (clinical),Genetics
Link
http://www.nature.com/articles/hdy198893.pdf
Reference30 articles.
1. Anderson, S M, and Mcdonald, J F. 1981a. A method for determining the in vivo stability of Drosophila alcohol dehydrogenase (EC 1.1.1.1.). Biochem Genet, 19, 411–419.
2. Anderson, S M, and Mcdonald, J F. 1981b. Effect of environmental alcohol on in vivo properties of Drosophila alcohol dehydrogenase. Biochem Genet, 19, 421–430.
3. Ayala, F J, Powell, J R, Tracey, M L, Mourão, C A, and Pérez-Salas, S. 1972. Enzyme variability in the Drosophila willistoni group. IV, Genie variation in natural populationsof Drosophila willistoni. Genetics, 70, 113–139.
4. Barbancho, M, S´nchez-Cañete, F J S, Dorado, G, and Pineda, M. 1987. Relation between tolerance to ethanol and alcohol dehydrogenase (ADH) activity in Drosophila melanogaster: Selection, genotype and sex effects. Heredity, 58, 443–450.
5. David, J R, Bocquet, C, Van Herrewege, J, Fouillet, P, and Arens, M F. 1978. Alcohol metabolism in Drosophila melanogaster: Uselessness of the most active aldehyde oxidase produced by the Aldox locus. Biochem Genet, 16, 203–211.
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