Genetic and biochemical aspects of trehalase and sucrase of Drosophila Melanogaster
Date
1977
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Abstract
There are three major forms of the enzyme trehalase (E.C~ 3.2.1.28) found in Drosophila melanogaster, a soluble abdominal form, a soluble muscle form and an insoluble) particulate, muscle form c The location of an area of the genome coding for the production of all three forms of the enzyme is proposed on the basis of enzyme determinations in a set of duplication and deletion bearing aneuploids exhibiting dosage sensitivity. This region lies between 55B and 55E on the right arm of chromosome two of the Drosophila genome. The localization of the structural gene of the enzyme sucrase (E.C. 3.2.1.26) is proposed on the basis of similar determinations. The sucrase structural gene lies between 31CD and 31EF on the left arm of chromosome two of the Drosophila genome. Polyacrylamide disc-gel electrophoresis reveals only one band of trehalase activity in crude homogenates of whole fly, thorax and abdomen preparations. Similarly only one peak of trehalase activity is seen when these extracts are run on isoelectrofocusing columns. Drosophila trehalase has an isoelectric point of 4.73 ± 0.02. Isoelectrofocusing of abdominal extracts reveals the existence of two sucrase components, one exhibiting an isoelectric point of 4.63 ± 0.02 and the other an iso electric point of 4.83 ± 0.02. This suggests that there are two forms of abdominal sucrase in Drosophi la. On the basis of these data it is concluded that the three forms of trehalase are manifestations of a single protein whose primary sequence is coded for by a single trehalase gene, designated Treh+. Similarly the two forms of abdominal sucrase derive from a common protein coded for by a single sucrase gene, designated Sucr+.
Description
Bibliography: p. 72-78.
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Citation
Oliver, M. J. (1977). Genetic and biochemical aspects of trehalase and sucrase of Drosophila Melanogaster (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/15946