Proteomic Analysis of Therapeutically Important Bacteriophage 812 by Combination of Electrophoresis and Mass Spectrometry

Result code in 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>

Result on the web

—

DOI - Digital Object Identifier

—

Result language

angličtina

Original language name

Proteomic Analysis of Therapeutically Important Bacteriophage 812 by Combination of Electrophoresis and Mass Spectrometry

Original language description

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

Czech name

Proteomic Analysis of Therapeutically Important Bacteriophage 812 by Combination of Electrophoresis and Mass Spectrometry

Czech description

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

Type

D - Article in proceedings

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

—

Project

<a href="/en/project/GA203%2F03%2F0515" target="_blank" >GA203/03/0515: Integrated genome and proteome analysis of therapeutically important bacteriophages by combination of electrophoresis and mass spectrometry</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2003

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Article name in the collection

Proceedings of the 51st Annual Conference on Mass Spectrometry and Allied Topics

ISBN

—

ISSN

—

e-ISSN

—

Number of pages

1

Pages from-to

1152

Publisher name

American Society for Mass Spectrometry

Place of publication

Montreal

Event location

Montreal, Canada

Event date

Jun 8, 2003

Type of event by nationality

WRD - Celosvětová akce

UT code for WoS article

—