Use of surface-enhanced laser desorption ionization–time-of-flight to identify heat shock protein 70 isoforms in closely related species of the virilis group of Drosophila
| Autor: | Olga G. Zatsepina, Peter Tornatore, Alexander Karavanov, V Shilova, Michael B. Evgen'ev, David G. Garbuz |
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| Rok vydání: | 2005 |
| Předmět: |
Hot Temperature
Short Communication Immunoblotting Biology Peptide Mapping Biochemistry Species Specificity Heat shock protein Animals Protein Isoforms Electrophoresis Gel Two-Dimensional HSP70 Heat-Shock Proteins Trypsin Heat shock Peptide sequence Gel electrophoresis Antibodies Monoclonal Genetic Variation Sequence Analysis DNA Cell Biology biology.organism_classification Molecular biology Surface-enhanced laser desorption/ionization Hsp70 Molecular Weight Isoelectric point Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Drosophila Electrophoresis Polyacrylamide Gel Drosophila melanogaster Heat-Shock Response |
| Zdroj: | Cell Stress & Chaperones. 10:12 |
| ISSN: | 1466-1268 1355-8145 |
| DOI: | 10.1379/csc-71.1 |
| Popis: | The 70-kDa heat shock protein (Hsp) family in all Drosophila species includes 2 environmentally inducible family members, Hsp70 and Hsp68. Two-dimensional gel electrophoresis revealed an unusual pattern of heat shock– inducible proteins in the species of the virilis group. Trypsin fingerprinting and microsequencing of tryptic peptides using ProteinChip Array technology identified the major isoelectric variants of Hsp70 family, including Hsp68 isoforms that differ in both molecular mass and isoelectric point from those in Drosophila melanogaster. The peculiar electrophoretic mobility is consistent with the deduced amino acid sequence of corresponding hsp genes from the species of the virilis group. |
| Databáze: | OpenAIRE |
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