Automating proteome analysis: improvements in throughput, quality and accuracy of protein identification by peptide mass fingerprinting

2004 ◽  
Vol 18 (23) ◽  
pp. 2785-2794 ◽  
Author(s):  
Ludovic Canelle ◽  
C�dric Pionneau ◽  
Arul Marie ◽  
Jordane Bousquet ◽  
Jean Bigeard ◽  
...  
Keyword(s):  
Protein Identification ◽  
Proteome Analysis ◽  
Peptide Mass Fingerprinting ◽  
Peptide Mass

scholarly journals Stable isotope labelling in vivo as an aid to protein identification in peptide mass fingerprinting

PROTEOMICS ◽  
2002 ◽  
Vol 2 (2) ◽  
pp. 157-163 ◽  
Author(s):  
Julie M. Pratt ◽  
Duncan H. L. Robertson ◽  
Simon J. Gaskell ◽  
Isabel Riba-Garcia ◽  
Simon J. Hubbard ◽  
...  
Keyword(s):  
Stable Isotope ◽  
Protein Identification ◽  
Peptide Mass Fingerprinting ◽  
Stable Isotope Labelling ◽  
Isotope Labelling ◽  
Peptide Mass

scholarly journals Hypoxic Response of Mycobacterium tuberculosis Studied by Metabolic Labeling and Proteome Analysis of Cellular and Extracellular Proteins

2002 ◽  
Vol 184 (13) ◽  
pp. 3485-3491 ◽  
Author(s):  
Ida Rosenkrands ◽  
Richard A. Slayden ◽  
Janne Crawford ◽  
Claus Aagaard ◽  
Clifton E. Barry ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Proteome Analysis ◽  
Peptide Mass Fingerprinting ◽  
Extracellular Proteins ◽  
Metabolic Labeling ◽  
Low Oxygen ◽  
Hypoxic Response ◽  
Peptide Mass ◽  
Oxygen Conditions

ABSTRACT The events involved in the establishment of a latent infection with Mycobacterium tuberculosis are not fully understood, but hypoxic conditions are generally believed to be the environment encountered by the pathogen in the central part of the granuloma. The present study was undertaken to provide insight into M. tuberculosis protein expression in in vitro latency models where oxygen is depleted. The response of M. tuberculosis to low-oxygen conditions was investigated in both cellular and extracellular proteins by metabolic labeling, two-dimensional electrophoresis, and protein signature peptide analysis by liquid chromatography-mass spectrometry. By peptide mass fingerprinting and immunodetection, five proteins more abundant under low-oxygen conditions were identified from several lysates of M. tuberculosis: Rv0569, Rv2031c (HspX), Rv2623, Rv2626c, and Rv3841 (BfrB). In M. tuberculosis culture filtrates, two additional proteins, Rv0363c (Fba) and Rv2780 (Ald), were found in increased amounts under oxygen limitation. These results extend our understanding of the hypoxic response in M. tuberculosis and potentially provide important insights into the physiology of the latent bacilli.

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