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A biochemical genetic study of alcohol dehydrogenase isozymes of the medfly,Ceratitis capitata wied
Authors:G. Gasperi  L. Baruffi  A. R. Malacrida  A. S. Robinson
Affiliation:(1) Department of Animal Biology, Laboratory of Zoology, University of Pavia, piazza Botta 9, I-27100 Pavia, Italy;(2) Institute of Molecular Biology and Biotechnology—Foundation of Research and Technology, Hellas, P.O. Box 1527, 711 10 Heraklion, Crete, Greece
Abstract:A concerted effort is under way to analyze, at the genetic, biochemical, and molecular level, theAdh gene system in the medflyCeratitis capitata, an important agricultural pest. The isoelectric focusing (IEF) pattern of alcohol dehydrogenase (ADH) of the medfly demonstrates the presence of two well-differentiated, genetically independent dimeric proteins, called ADH-1 and ADH-2. These proteins do not exhibit interlocus heterodimeric isozymes, and the genes are not controlled coordinately during development,Adh 1 andAdh 2 being expressed mainly in muscle or in fat body and ovary, respectively. From the intensity of the IEF isozyme patterns, primary alcohols are judged to be better substrates than secondary alcohols, in contrast withDrosophila melanogaster ADH, and ethanol is probably the most efficient substrate for both sets of isozymes. The isoelectric points of ADH-1 (pI=5.4) and ADH-2 (pI=8.6) are different fromD. melanogaster ADH (pI=7.6), but the medfly ADH-1 has a native molecular weight (approx. 58 kD) close to that ofD. melanogaster. A population survey of samples both from laboratory strains and from wild geographically different populations showed that theAdh 1 locus is more polymorphic thanAdh 2. The most variable populations are from Africa, the supposed source area of the species. Further, a case of selection at theAdh 1 locus under laboratory conditions is reported. The hypothesis ofAdh gene duplication and the degree of similarity between medfly andDrosophila ADH are also discussed. This research was supported mainly by National Research Council of Italy, Special Project RAISA, Sub-project No. 2, Paper No. 342. Grants from the International Atomic Energy Agency, Vienna, Austria, from European Communities Commission, Second R & D Programme, “Science and Technology for Development,” and from the Italian Ministry of University and Scientific Research and Technology (“Funds 40%”) also supported this work. This paper was written when the senior author was on leave of absence at the IMBB, Crete, Greece; he was financially supported by an ECC Senior Fellowship.
Keywords:alcohol dehydrogenase isozymes (ADH)  biochemical features of gene products  differential expression of duplicated loci  genetic polymorphism   Ceratitis capitata (medfly)
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