Characterization of the Protein Subset Desorbed by MALDI from Whole Bacterial Cells

• Published in: Analytical chemistry (Washington) Vol. 73; no. 4; pp. 746 - 750
• Main Authors: Ryzhov, Victor, Fenselau, Catherine
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 15-02-2001
• Subjects: Analytical, structural and metabolic biochemistry; Bacteria; Bacterial Proteins - chemistry; Bacteriological methods and techniques used in bacteriology; Bacteriology; Biochemistry; Biological and medical sciences; Cells; Chemistry; Cold Temperature; Databases, Factual; Escherichia coli - chemistry; Fundamental and applied biological sciences. Psychology; General aspects, investigation methods; Microbiology; Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Analysis method; Escherichia coli; Database; Bacteria; Identification; Matrix assisted laser desorption ionization; Mass spectrometry; Protein; Enterobacteriaceae
• ISSN: 0003-2700; 1520-6882
• DOI: 10.1021/ac0008791

This study characterizes various features of the proteins that are detected in MALDI mass spectra when whole bacteria cells are analyzed, in an effort to understand why some proteins are successfully detected and many others are not. Forty peaks observed in the mass range 4000−20 000 Da in the spectra of Escherichia coli K-12 and 11775 are tentatively assigned to proteins in a protein database, and these proteins are characterized by cell location, copy number, pI, and hydropathicity. Those detected originate in the cytosol and generally share the traits of high abundance within the cell, strong bacisity, and medium hydrophilicity.