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Determination of Bacterial Protein Profiles by Matrix‐assisted Laser Desorption/Ionization Mass Spectrometry with High‐performance Liquid Chromatography
Author(s) -
Liang Xiaoli,
Zheng Kefei,
Qian Masrk G.,
Lubman David M.
Publication year - 1996
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/(sici)1097-0231(19960731)10:10<1219::aid-rcm660>3.0.co;2-r
Subject(s) - chemistry , chromatography , mass spectrometry , matrix assisted laser desorption/ionization , desorption , surface enhanced laser desorption/ionization , capillary action , matrix (chemical analysis) , analytical chemistry (journal) , high performance liquid chromatography , protein mass spectrometry , tandem mass spectrometry , adsorption , materials science , organic chemistry , composite material
A rapid method for profiling bacterial and cellular proteins has been developed using a combination of capillary high‐performance liquid chromatography separation followed by (MALDI‐MS) matrix‐assisted laser desorption/ionization mass spectrometric analysis. In this method, bacteria are sonicated, the cell walls broken, and the water‐soluble proteins precipitated for analysis. The proteins are separated by capillary liquid chromatography and detected on‐line by a UV absorption detector. The eluents are then collected for off‐line analysis by MALDI‐MS. Using this method, it is demonstrated that bacteria can be discriminated based upon their protein profiles to the species level with only pmol level detection of proteins. It has also proved to be a fast and accurate means for monitoring the expression of Hsp27 in an insect cell system.