A biochemical genetic study of alcohol dehydrogenase isozymes of the medfly, Ceratitis capitata Wied

A concerted effort is under way to analyze, at the genetic, biochemical and molecular level, the Adh gene system in the medfly; Ceratitis capitata, all important agricultural pest. The isoelectric focusing (IEF) pattern of alcohol dehydrogenase (ADH) of the medfly demonstrates the presence of two we...

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Bibliographic Details
Published in:Biochemical genetics 1992-06, Vol.30 (5/6), p.289-304
Main Authors: Gasperi, G. (University of Pavia, Pavia, Italy), Baruffi, L, Malacrida, A.R, Robinson, A.S
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Alcohol Dehydrogenase - genetics
Alcohol Dehydrogenase - metabolism
ALCOHOL DESHIDROGENASA
ALCOOL DESHYDROGENASE
Animals
Biological and medical sciences
CERATITIS CAPITATA
CERDENA
Classical genetics, quantitative genetics, hybrids
DESARROLLO BIOLOGICO
DEVELOPPEMENT BIOLOGIQUE
Diptera - enzymology
Diptera - genetics
Drosophila melanogaster - enzymology
Electrophoresis, Polyacrylamide Gel
ENZIMAS
ENZYME
EXPRESION GENICA
EXPRESSION DES GENES
Fundamental and applied biological sciences. Psychology
GENE
Gene Expression
GENES
Genetic Variation
Genetics of eukaryotes. Biological and molecular evolution
GUATEMALA
Invertebrata
Isoelectric Focusing
ISOELECTROFOCALISATION
ISOELECTROFOQUE
ISOENZIMAS
ISOENZYME
Isoenzymes - genetics
Isoenzymes - metabolism
KENIA
KENYA
LOCI
LOCUS
Molecular Weight
POLIMORFISMO BIOQUIMICO
POLIMORFISMO GENETICO
POLYMORPHISME BIOCHIMIQUE
POLYMORPHISME GENETIQUE
PROPIEDADES FISICO-QUIMICAS
PROPRIETE PHYSICOCHIMIQUE
REUNION
SARDAIGNE
SELECCION
SELECTION
Substrate Specificity
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Summary:A concerted effort is under way to analyze, at the genetic, biochemical and molecular level, the Adh gene system in the medfly; Ceratitis capitata, all 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, Adh1 and Adh2 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 with Drosophila 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 from D. melanogaster ADH (pI = 7.6), but the medfly ADH-1 has a native molecular weight (approx. 58 kD) close to that of D. melanogaster. A population survey of samples both from laboratory strains and from wild geographically different populations showed that the Adh1 locus is more polymorphic than Adh2. The most variable populations are from Africa, the supposed source area of the species. Further, a case of selection at the Adh1 locus under laboratory conditions is reported. The hypothesis of Adh gene duplication and the degree of similarity between medfly and Drosophila ADH are also discussed
ISSN:0006-2928
1573-4927
DOI:10.1007/BF02396218