HIGH RESOLUTION LIQUID CHROMATOGRAPHIC MASS SPECTROMETRIC IDENTIFICATION OF PEPTIDES USING ELECTROSPRAY IONIZATION

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Authors
  1. Hancock, J.R.
  2. D'Agostino, P.A.
  3. Provost, L.
  4. Semchuk, P.D.
  5. Hodges, R.S.
Corporate Authors
Defence Research Establishment Suffield, Ralston ALTA (CAN);Alberta Univ, Edmonton ALTA (CAN) Dept of Biochemistry
Abstract
High resolution liquid chromatography electrospray mass spectrometry (LC-ESI-MS) was investigated for the identification of known and unknown peptides in a research effort designed to evaluate the applicability of this and complementary MS techniques for the characterization and identification of peptides. The monoisotopic molecular weights of five related peptides with molecular weights between 2000 and 2500 Da, typical of bioactive peptides, were acquired with a magnetic sector resolution of 300 (10% valley definition). Tryptic maps were generated for each peptide during high resolution LC-ESI-MS analysis and collisionally activated dissociation (CAD) in the ESI interface resulted in the production of characteristic product ions that enabled amino acid sequencing of the tryptic fragments. Under narrow and wide mass range magnetic sector scanning conditions monoisotopic molecular weight errors were typically in the 10-20 and 30-40 ppm range, respectively. Unknown identification, a critical requirement for MS methods developed in support of chemical/biological sample analysis, was demonstrated during analysis of an incomplete synthetic peptide reaction mixture. The reaction mixture for the peptide, LTTAVKKVLTTGLPALIS, was selected since the 18 amino acid target peptide was not synthesized. In its place were a number of lower molecular weight unknown peptides. TRUNCATED
Keywords
Electrospray mass spectrometry;Tandem mass spectrometry;High resolution
Report Number
DRES-638 —
Date of publication
01 Nov 1996
Number of Pages
35
DSTKIM No
97-01366
CANDIS No
501783
Format(s):
Hardcopy;Document Image stored on Optical Disk

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