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Chemistry, Mass Spectrometry and Peptide-Mass Databases: Evolution of Methods for the Rapid Identification and Mapping of Cellular Proteins

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Abstract

Large-format 2D gel electrophoresis systems have been developed that are capable of resolving several thousand cellular proteins in a matter of days [1,2]. For a number of years, a combination of Edman microsequence analysis and identification of proteins by staining with specific antibodies has been used to systematically categorize proteins and establish cellular databases [35]. There are, however, significant problems associated with these approaches. Most resolved proteins are only present in the low- to upper-femtomole range, significantly below the level at which automated sequencers can reliably operate [6, 7]. The relatively slow speed of the Edman process (one or two samples per machine per day) also means that the sheer number of proteins is too great to permit large-scale characterization within any useful period of time. The use of monoclonal antibodies, whilst both rapid and extremely sensitive, requires the ready availability of a large pool of antibody probes.

Keywords

  • Tryptic Peptide
  • Thionyl Chloride
  • Octyl Glucoside
  • Heptafluorobutyric Acid
  • Imperial Cancer Research Fund

These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Pappin, D.J.C., Rahman, D., Hansen, H.F., Bartlet-Jones, M., Jeffery, W., Bleasby, A.J. (1996). Chemistry, Mass Spectrometry and Peptide-Mass Databases: Evolution of Methods for the Rapid Identification and Mapping of Cellular Proteins. In: Burlingame, A.L., Carr, S.A. (eds) Mass Spectrometry in the Biological Sciences. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-4612-0229-5_7

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  • DOI: https://doi.org/10.1007/978-1-4612-0229-5_7

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