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Purification and cDNA Cloning of the Alcohol Dehydrogenase of the Flesh Fly Sarcophaga peregrine
A Structural Relationship between Alcohol Dehydrogenase and a 25-kDa Protein
Article first published online: 31 AUG 2004
DOI: 10.1111/j.1432-1033.1996.0698p.x
1742-4658/asset/cover.gif?v=1&s=fc98a9fc84ccc5e1b83463cabb40f397544364eb "European Journal of Biochemistry")
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How to Cite
Horio, T., Kubo, T. and Natori, S. (1996), Purification and cDNA Cloning of the Alcohol Dehydrogenase of the Flesh Fly Sarcophaga peregrine. European Journal of Biochemistry, 237: 698–703. doi: 10.1111/j.1432-1033.1996.0698p.x
Publication History
- Issue published online: 31 AUG 2004
- Article first published online: 31 AUG 2004
- (Received 31 January 1996) – EJB 960132/4
- Abstract
- Article
- References
- Cited By
Keywords:
- insect;
- alcohol dehydrogenase;
- molecular evolution
We purified to homogeneity two proteins with molecular masses of 25 kDa from the fat body of the Sarcophaga larva. One was alcohol dehydrogenase (ADH) and the other was a 25-kDa protein of which the genomic DNA had been cloned. We isolated the cDNA for ADH and determined its amino acid sequence. Amino acid sequence identity between ADH and the 25-kDa protein was 40%, indicating that they are structurally related proteins. The amount of ADH in Sarcophaga was almost constant through the larval stage to the adult stage, but the 25-kDa protein was detected only within a restricted period between the final larval instar and the early pupal stage.