Only one molecular form of trehalase (E.C. 3.2.1.28) was detectable in adult Drosophila melanogaster by polyacrylamide gel electrophoresis and isoelectric focusing. An examination of duplication- and deletion-bearing aneuploids exhibiting dosage sensitivity indicated that the enzyme is encoded by a
Genetic and biochemical aspects of sucrase fromDrosophila melanogaster
โ Scribed by Melvin J. Oliver; John H. Williamson
- Publisher
- Springer
- Year
- 1979
- Tongue
- English
- Weight
- 487 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-2928
No coin nor oath required. For personal study only.
โฆ Synopsis
Isoelectrofocusing of abdominal extracts of Drosophila melanogaster revealed the existence of two forms of sucrase (E.C. 3.2.1.26). One form exhibited an isoelectric point of 4.63 +/- 0.02 while the other form exhibited an isoelectric point of 4.83 +/- 0.02. The localization of the structural gene for sucrase is proposed on the basis of enzyme determinations in a series of duplication- and deletion-bearing aneuploids. We suggest that the sucrase structural gene lies between 31CD and 31EF on the left arm of chromosome 2 and that the two forms of abdominal sucrase derive from a common protein coded for by a single sucrase gene designated Sucr+.
๐ SIMILAR VOLUMES
Phosphofructokinase (PFK;EC 2.7.1.11) activity in Drosophila melanogaster is controlled by a single dosage-sensitive region of the genome between 45F and 47E of chromosome IIR. Only a single form of PFK was detected electrophoretically in both adults and larvae. Nearly 90% of the PFK activity in adu
The molecular weight forms of kynuren&e formamidase were studied both genetically and biochemically. Formamidase I (native molecular weight 60,000) was purified using ( NH4 ) 2 S04 and p H fractionation, D EAE-cellulose chromatography at two different pH's, hydroxylapatite chromatography, and Sephad
Glutamate dehydrogenase has been purified to near-homogeneity from mature larvae of Drosophila melanogaster. The enzyme has a molecular weight of 347,000 measured by sucrose gradient sedimentation and 343,000 measured by variable-porosity acrylamide gel electrophoresis. Electrophoresis under denatur