Part II: defining and quantifying individual and co-cultured intracellular proteomes of two thermophilic microorganisms by GeLC-MS² and spectral counting

Probing the intracellular proteome of Thermotoga maritima and Caldicellulosiruptor saccharolyticus in pure and co-culture affords a global investigation into the machinery and mechanisms enduring inside the bacterial thermophilic cell at the time of harvest. The second of a two part study, employing...

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Veröffentlicht in:	Analytical and bioanalytical chemistry 2010-09, Vol.398 (1), p.391-404
Hauptverfasser:	Muddiman, David, Andrews, Genna, Lewis, Derrick, Notey, Jaspreet, Kelly, Robert
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical Chemistry Applied sciences Bacteria Bacterial Proteins - analysis Bacterial Proteins - metabolism Biochemistry Caldicellulosiruptor Caldicellulosiruptor saccharolyticus Characterization and Evaluation of Materials Chemistry Chemistry and Materials Science Chemotaxis Chromatography, Liquid Co-cultivation Coculture Techniques Counting Culture Durability Electrophoresis, Polyacrylamide Gel Exact sciences and technology Focusing Food Science Fourier Analysis GeLC-MS Global environmental pollution Gram-Positive Bacteria - growth & development Gram-Positive Bacteria - metabolism Indication Intracellular proteome Intracellular Space - metabolism Laboratory Medicine Microorganisms Monitoring/Environmental Analysis Original Paper Pollution Proteins Proteome - analysis Spectra Spectral counting Spectrometry, Mass, Electrospray Ionization Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Spectrum Analysis - statistics & numerical data Temperature Thermotoga maritima Thermotoga maritima - growth & development Thermotoga maritima - metabolism
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Zusammenfassung:	Probing the intracellular proteome of Thermotoga maritima and Caldicellulosiruptor saccharolyticus in pure and co-culture affords a global investigation into the machinery and mechanisms enduring inside the bacterial thermophilic cell at the time of harvest. The second of a two part study, employing GeLC-MS² a variety of proteins were confidently identified with
ISSN:	1618-2642 1618-2650
DOI:	10.1007/s00216-010-3929-8