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Your search keyword '"Corrado Caggese"' showing total 3 results
Start Over Author "Corrado Caggese" Journal biochemical genetics
3 results on '"Corrado Caggese"'

1. Purification and genetic control of NAD-dependent glutamate dehydrogenase from Drosophila melanogaster

Author

A. Ferrandino, V. De Pinto, and Corrado Caggese

Subjects
Male, Macromolecular Substances, Biochemistry, Chromosomes, Gene mapping, Glutamate Dehydrogenase, Genetics, Animals, Molecular Biology, Polyacrylamide gel electrophoresis, Ecology, Evolution, Behavior and Systematics, Crosses, Genetic, chemistry.chemical_classification, biology, Glutamate dehydrogenase, Structural gene, Chromosome, General Medicine, biology.organism_classification, NAD, Molecular biology, Molecular Weight, Electrophoresis, Enzyme, Drosophila melanogaster, chemistry, Genes, Larva, Female
Abstract

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 denaturing conditions showed that the enzyme consists of six subunits of molecular weight 57,000. The structural gene for GDH has been mapped at 81.7 +/- 0.8 on the third chromosome by means of an electrophoretic variant.

Published
1982

2. Purification of the glutamine synthetase II isozyme of Drosophila melanogaster and structural and functional comparison of glutamine synthetases I and II

Author

Corrado Caggese, G Prezioso, Ferruccio Ritossa, and V. De Pinto

Subjects
Macromolecular Substances, Protein subunit, Biology, Biochemistry, Isozyme, Peptide Mapping, Chromatography, DEAE-Cellulose, Glutamate-Ammonia Ligase, Glutamine synthetase, Genetics, Transferase, Animals, Molecular Biology, Polyacrylamide gel electrophoresis, Ecology, Evolution, Behavior and Systematics, chemistry.chemical_classification, General Medicine, Molecular biology, Glutamine, Isoenzymes, Molecular Weight, Enzyme, Isoelectric point, Drosophila melanogaster, chemistry, Electrophoresis, Polyacrylamide Gel
Abstract

Glutamine synthetase II was purified from Drosophila melanogaster adults. It was completely separable from the isozyme glutamine synthetase I by means of DEAE chromatography. The complete enzyme has an apparent molecular weight of 360,000. After two-dimensional electrophoresis it gave a single molecular species with an apparent molecular weight of 42,000. Structural analysis of the two isozymes showed that they are different both in subunit molecular weight and in isoelectric point. Peptide maps of the purified subunits showed considerable dissimilarity. Glutamine synthetase II is more active than glutamine synthetase I in the transferase assay, while the opposite is true in the biosynthetic assay. The kinetic parameters were determined, showing again noteworthy differences between the two isozymes. We therefore conclude that two forms of glutamine synthetase are present in Drosophila, with different primary structures, different kinetic behavior, and the possibility of different functional properties.

Published
1987

3. Genetic determinants of glutamine synthetase in Drosophila melanogaster: a gene for glutamine synthetase I resides in the 21B3-6 region

Author

Ferruccio Ritossa, Z Paolo Barsanti, Maria Pia Bozzetti, Ruggiero Caizzi, Corrado Caggese, Caggese, C., Caizzi, R, Bozzetti, Maria Giuseppina, Barsanti, P., and Ritossa, F.

Subjects
Male, Ethyl methanesulfonate, allozyme, medicine.disease_cause, Biochemistry, chemistry.chemical_compound, Gene mapping, Glutamate-Ammonia Ligase, Glutamine synthetase, Genetics, medicine, Animals, Deletion mapping, Molecular Biology, Ecology, Evolution, Behavior and Systematics, Crosses, Genetic, Mutation, biology, Chromosome Mapping, General Medicine, biology.organism_classification, Null allele, Molecular biology, Complementation, Drosophila melanogaster, chemistry, Genes, null allele, glutamine synthetase I, Drosophila, Female, genetic mapping
Abstract

Recombinational and deletion mapping of electrophoretic variants of the glutamine synthetase I isozyme (GSI) in Drosophila melanogaster locates the gene in the 21B region on the second chromosome. We have conducted a genetic analysis of the region extending cytologically from 21A to 21B4-6. Recessive lethal mutations were generated by ethyl methanesulfonate (EMS) and ethyl nitrosourea (ENU) mutagenesis and by hybrid dysgenesis (HD). These lethals fall into seven functional groups, which were partially ordered by complementation with cytologically defined deficiencies of this region generated by hybrid dysgenesis. Two of the EMS- and two of the ENU-induced lethals fulfill biochemical criteria expected for null alleles of the GSI gene.

Published
1988

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