Sequence Analysis of Polypeptides by Direct Chemical Ionization Mass Spectrometry
The identification and structural elucidation of small, biologically active peptides is a challenging analytical problem. These compounds are often not amenable to classical protein sequencing methods because of the presence of N-terminal blocking groups, carbohydrate side chains, or covalently modified amino acids. The low volatility and thermal lability of most polypeptides requires that they be derivatized prior to conventional electron impact (EI) or chemical ionization (CI) mass spectrometry for complete structural evaluation (1). Unfortunately, peptides of biological origin are often obtainable only in sub-nanomole amounts which makes sample consuming derivatization highly undesirable. Furthermore, chemical treatment may modify or destroy sensitive functional groups present in the peptide.
KeywordsChemical Ionization Mass Spectrometry Modify Amino Acid Field Desorption Coated Wire Carbohydrate Side Chain
Unable to display preview. Download preview PDF.
- 1).Biemann, K. (1980) in Biochemical Applications of Mass Spectrometry, First Supplementary Volume (Waller, G.R., and Dermer, O.C., eds) pp. 469–525, Wiley Interscience, New York.Google Scholar
- 2).Beckey, H.D. (1977) Principles of Field Ionization and Field Desorption Mass Spectrometry, Pergamon Press, Oxford.Google Scholar
- Macfarlane, R.D. (1980) in Biochemical Applications of Mass Spectrometry, First Supplementary Volume (Waller, G.R., and Dermer, O.C., eds) pp. 1209–1218, Wiley Interscience, New York.Google Scholar
- 9).Reinhold, V.N. and Carr, S.A. (1981), submitted to Anal. Chem.Google Scholar