Proteomic Analysis of Therapeutically Important Bacteriophage 812 by Combination of Electrophoresis and Mass Spectrometry
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00008100" target="_blank" >RIV/00216224:14310/03:00008100 - isvavai.cz</a>
Výsledek na webu
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DOI - Digital Object Identifier
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Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Proteomic Analysis of Therapeutically Important Bacteriophage 812 by Combination of Electrophoresis and Mass Spectrometry
Popis výsledku v původním jazyce
The alarming increase in antibiotic-resistant bacteria has renewed interest in bacteriophage therapy of various human infections, such as postoperative staphylococcal wound infections or anthrax. Genetic engineering has been previously applied for obtaining phage mutants with the desired host specificity. However, the genomic sequence similarity of the different phages is generally low, and identification of proteins with the same function in various phages based solely on the DNA sequence is often impossible. Furthermore, amino acid modifications, such as variants and post-translational modifications of the predicted proteins cannot be deduced from the DNA sequence. In this work, we propose new approaches to the analysis of the phage proteins, especially low abundant proteins, such as lytic enzymes. SDS gel electrophoresis was used for the protein separation followed by tryptic digestion and ESI or MALDI analysis. Additionally, protein and peptide separations were performed with capil
Název v anglickém jazyce
Proteomic Analysis of Therapeutically Important Bacteriophage 812 by Combination of Electrophoresis and Mass Spectrometry
Popis výsledku anglicky
The alarming increase in antibiotic-resistant bacteria has renewed interest in bacteriophage therapy of various human infections, such as postoperative staphylococcal wound infections or anthrax. Genetic engineering has been previously applied for obtaining phage mutants with the desired host specificity. However, the genomic sequence similarity of the different phages is generally low, and identification of proteins with the same function in various phages based solely on the DNA sequence is often impossible. Furthermore, amino acid modifications, such as variants and post-translational modifications of the predicted proteins cannot be deduced from the DNA sequence. In this work, we propose new approaches to the analysis of the phage proteins, especially low abundant proteins, such as lytic enzymes. SDS gel electrophoresis was used for the protein separation followed by tryptic digestion and ESI or MALDI analysis. Additionally, protein and peptide separations were performed with capil
Klasifikace
Druh
D - Stať ve sborníku
CEP obor
EB - Genetika a molekulární biologie
OECD FORD obor
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Návaznosti výsledku
Projekt
<a href="/cs/project/GA203%2F03%2F0515" target="_blank" >GA203/03/0515: Integrovaná analýza genomu a proteomu terapeuticky významných bakteriofágů kombinací elektroforézy a hmotnostní spektrometrie</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2003
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název statě ve sborníku
Proceedings of the 51st Annual Conference on Mass Spectrometry and Allied Topics
ISBN
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ISSN
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e-ISSN
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Počet stran výsledku
1
Strana od-do
1152
Název nakladatele
American Society for Mass Spectrometry
Místo vydání
Montreal
Místo konání akce
Montreal, Canada
Datum konání akce
8. 6. 2003
Typ akce podle státní příslušnosti
WRD - Celosvětová akce
Kód UT WoS článku
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