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Variation in the biochemical properties of the Drosophila alcohol dehydrogenase allozymes

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Abstract

Thirteen Drosophila Adh variants have been characterized with respect to gene expression, substrate preference, thermostability, and specific activity. The results suggest that the variants may be grouped into two biochemical classes, typified by the properties of the two most common enzyme forms, ADH-F and ADH-S. Membership of these classes cannot be predicted from electrophoretic mobility, nor is any simple classification possible with regard to the characteristics of level of gene expression (in terms of ADH activity or ADH protein) or thermostability of the gene product.

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Author notes

  1. Geoffrey K. Chambers

    Present address: Museum of Comparative Zoology, Harvard University, 02138, Cambridge, Massachusetts

Authors and Affiliations

  1. Department of Population Biology, Research School of Biological Sciences, Australian National University, 2601, Canberra, ACT, Australia

    Geoffrey K. Chambers, Ann V. Wilks & John B. Gibson

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  1. Geoffrey K. Chambers
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  2. Ann V. Wilks
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  3. John B. Gibson
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Chambers, G.K., Wilks, A.V. & Gibson, J.B. Variation in the biochemical properties of the Drosophila alcohol dehydrogenase allozymes. Biochem Genet 22, 153–168 (1984). https://doi.org/10.1007/BF00499295

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  • DOI: https://doi.org/10.1007/BF00499295

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