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Studies of esterase 6 inDrosophila melanogaster. I. The genetics of a posttranslational modification

✍ Scribed by Bruce J. Cochrane; Rollin C. Richmond


Publisher
Springer
Year
1979
Tongue
English
Weight
877 KB
Volume
17
Category
Article
ISSN
0006-2928

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✦ Synopsis


A locus has been found, an allele of which causes a modification of some allozymes of the enzyme esterase 6 in Drosophila melanogaster. There are two alleles of this locus, one of which is dominant to the other and results in increased electrophoretic mobility of affected allozymes. The locus responsible has been mapped to 3-56.7 on the standard genetic map (Est-6 is at 3-36.8). Of 13 other enzyme systems analyzed, only leucine aminopeptidase is affected by the modifier locus. Neuraminidase incubations of homogenates altered the electrophoretic mobility of esterase 6 allozymes, but the mobility differences found are not large enough to conclude that esterase 6 is sialylated.


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From analysis of the properties of the "pupal" esterase (p-esterase) in Drosophila virilis, it is concluded that it is heat stable, its electrophoretic detection depends on culture density, its expression is stage specific, and it is not a variant of esterase 2. It was also demonstrated that p-ester