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
Genetic and biochemical characterization of phosphofructokinase fromDrosophila melanogaster
โ Scribed by Lori R. Munneke; Glen E. Collier
- Publisher
- Springer
- Year
- 1985
- Tongue
- English
- Weight
- 549 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0006-2928
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โฆ Synopsis
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 adults is localized to the thorax. Purification of the enzyme was hampered by the extreme lability of Drosophila PFK; however, a 36-fold partial purification was achieved.
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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
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