From genome to proteome: protein map of Haemophilus influenzae.
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.
Langen
H
H
Gene Technologies, F. Hoffmann-La Roche Ltd., Pharmaceutical Research, Basel, Switzerland. hanno.langen@roche.com
Gray
C
C
Röder
D
D
Juranville
J F
JF
Takacs
B
B
Fountoulakis
M
M
D000596:Amino Acids; D001426:Bacterial Proteins / Q000032:analysis*; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D016680:Genome, Bacterial; D006193:Haemophilus influenzae / Q000737:chemistry*; D007526:Isoelectric Point; D013058:Mass Spectrometry / Q000379:methods; D010449:Peptide Mapping
D000596:Amino Acids; D001426:Bacterial Proteins