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From genome to proteome: Protein map of Haemophilus influenzae
Author(s) -
Langen Hanno,
Gray Chris,
Röder Daniel,
Juranville JeanFrançois,
Takacs Béla,
Fountoulakis Michael
Publication year - 1997
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150180727
Subject(s) - peptide mass fingerprinting , proteome , haemophilus influenzae , peptide , amino acid , two dimensional gel electrophoresis , bottom up proteomics , chemistry , lysis , computational biology , genome , gel electrophoresis , peptide sequence , biochemistry , biology , gene , chromatography , mass spectrometry , proteomics , tandem mass spectrometry , protein mass spectrometry , antibiotics
High‐resolution two‐dimensional (2‐D) polyacrylamide gel electrophoresis allows the separation of complex biological mixtures ( i.e. , several hundred proteins from a bacterial cell lysate) in a single experiment. In this report proteins from Haemophilus influenzae were separated by 2‐D gels and analyzed by peptide mass fingerprinting and/or amino acid analysis. By comparing the peptide mass profiles and the amino acid composition with the Haemophilus influenzae database, 119 protein spots were identified. The combination of amino acid analysis and peptide mass fingerprinting is a powerful tool for a rapid and economical identification of a large number of proteins resolved by 2‐D gels. Studies on gene regulation and changes of protein expression upon drug treatment require quick and serial analysis techniques to efficiently identify potential new drug targets.