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Competitive Peptide Adsorption to Nitrocellulose Covered Backing Material in Cf-252-Plasma Desorption Mass Spectrometry

  • G. Allmaier
  • E. Pittenauer
  • E. R. Schmid
Part of the NATO ASI Series book series (NSSB, volume 269)

Abstract

Cf-252-Plasma desorption (PD) [1] and Fast atom bombardment (FAB) [2] mass spectrometry have emerged as powerful tools for the analysis of complex underivatized peptide mixtures obtained from chemical or enzymatic cleaved proteins. It is well known that suppression effects in FAB mass spectra of tryptic peptide mixtures are limiting the use of this technique [3]. This perferential desorption/ionization was mainly attributed to the different hydrophobicity of the individual compounds [4]. In fact, it turned out that the different surface excess concentrations of the individual peptides in the applied liquid matrix were responsible for the selective desorption behavior [5]. This behavior of the tryptic peptides in the mixture was correlated with their average hydrophobicities [4,5] based either on the indices of Bull and Breese [6] or of Park et al. [7]. This severe limitation can be partly reduced by HPLC separation or chemical derivatization [4].

Keywords

Peptide Mixture Bovine Insulin Cyanogen Bromide Fast Atom Bombardment Mass Spectrometry Fission Event 
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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References

  1. 1.
    Torgerson D.F., Skowronski R.P. and Macfarlane R.D., Biochem. Biophys. Res. Commun. 60, 616 (1974).CrossRefGoogle Scholar
  2. 2.
    Barber M., Bordoli R.S., Sedgwick R.D. and Tyler A.N., J. Chem. Soc. Chem. Commun., 325 (1981).Google Scholar
  3. 3.
    Clench M.R., Garner G.V., Gordon D.B. and Barber M., Biomed. Mass Spectrom. 12, 355 (1985).CrossRefGoogle Scholar
  4. 4.
    Naylor S., Findeis A.F., Gibson B.W. and Williams D.H., J. Amer. Chem. Soc. 108, 6359 (1986).CrossRefGoogle Scholar
  5. 5.
    Allmaier G., Anal. Chim. Acta 223, 349 (1989).CrossRefGoogle Scholar
  6. 6.
    Bull H.B. and Breese K., Arch. Biochem. Biophys. 161, 665 (1974).CrossRefGoogle Scholar
  7. 7.
    Parker J.M.R., Guo D. and Hodges R.S., Biochemistry 25, 5425 (1986).CrossRefGoogle Scholar
  8. 8.
    Tsarbopoulus A., Becker G.W., Occolowitz J.L. and Jardine L, Anal. Biochem. 171, 113 (1988).CrossRefGoogle Scholar
  9. 9.
    Nielsen P.F., Roepstorff P., Clausen LG., Jensen E.B., Jonassen I., Svendsen A., Ballschmidt P. and Hansen F.B., Protein Engineering 2, 449 (1989).CrossRefGoogle Scholar
  10. 10.
    Allmaier G., Nam J.Y., Pittenauer E. and Schmid E.R., presented at the 2nd Int. Sympos. Mass Spectrometry in Health and Life Sciences, San Francisco, August 1989, 83.Google Scholar
  11. 11.
    Chen L., Cotter R.J. and Stults J.T., Anal. Biochem. 183, 190 (1989).CrossRefGoogle Scholar
  12. 12.
    Nielsen P.F. and Roepstorff P., Biomed. Environ. Mass Spectrom. 18, 131 (1989).CrossRefGoogle Scholar
  13. 13.
    Jonsson G., Hedin A., Sundqvist B., Saeve G., Nielsen P.F., Roepstorff P., Johansson K.E., Kamensky I. and Lindberg M., Anal. Chem. 58, 1048 (1986).CrossRefGoogle Scholar
  14. 14.
    Meek J.L., Proc. Natl. Acad. Sci. 77, 1632 (1980).ADSCrossRefGoogle Scholar
  15. 15.
    Allen G. in Sequencing of Proteins and Peptides ed. by Work T.S. and Burdon R.H., Elsevier, Amsterdam, NL (1981).Google Scholar
  16. 16.
    Gross E. and Witkop B., J. Biol. Chem. 237, 1956 (1962).Google Scholar
  17. 17.
    Glazer A.N., Delange RJ. and Sigman D.S. in Chemical Modification of Proteins, ed. by Work T.S. and Work E., Elsevier, Amsterdam, NL (1975).Google Scholar
  18. 18.
    Friedman M., Krull L.H. and Cavins J.F., J. Biolog. Chem. 245, 3868 (1970).Google Scholar
  19. 19.
    Roepstorff P., Nielsen P.F., Klarskov K., and Hojrup P., in The Analysis of Peptides and Proteins by Mass Spectrometry, ed. by McNeal C.J., Wiley, Chichester, GB (1988).Google Scholar
  20. 20.
    Chait B.T. and Field F.H., Biochem., Biophys. Res. Commun. 134, 420 (1986).CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • G. Allmaier
    • 1
  • E. Pittenauer
    • 1
  • E. R. Schmid
    • 1
  1. 1.Institute for Analytical ChemistryUniversity of ViennaViennaAustria

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