ANALYSIS OF BIOACTIVE PEPTIDES BY LIQUID CHROMATOGRAPHY - HIGH RESOLUTION ELECTROSPRAY MASS SPECTROMETRY

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Authors
  1. D'Agostino, P.A.
  2. Hancock, J.R.
  3. Provost, L.R.
Corporate Authors
Defence Research Establishment Suffield, Ralston ALTA (CAN)
Abstract
LC-high-resolution electrospray ionization (ESI)-MS data for a number of bioactive peptides, including substance P and bradykinins were acquired over a wide mass range by scanning the magnetic sector and calibrating externally with polyethylene glycol standards. Multiply charged ions were observed and errors between observed and theoretical monoisotopic molecular masses were typically in the 5 to 30 ppm range for the peptides during LC-ESI-MS and ESI-MS operation with magnetic sector resolutions between 2500 and 6000 (10% valley definition). Under collisionally activated dissociation conditions bn - and yn - series sequence ions were generally observed, enabling amino acid sequencing and the differentiation of lysine from glutamine, two amino acids differing in residue mass by only 0.0364 u. Mass accuracy was evaluated during an international round robin analytical exercise where the molecular masses of five unknown peptides were to be accurately determined. Isotopic clusters for charge states of up to +6 were fully resolved, facilitating the rapid and unambiguous assignment of charge states and calculation of monoisotopic molecular masses. Errors between theoretical and observed monoisotopic molecular masses were in the 2 to 18 ppm range for the five unknown peptides.
Keywords
Electrospray ionization;Electrospray mass spectrometry
Date of publication
10 Dec 1996
Number of Pages
12
Reprinted from
Journal of Chromatography, vol A 767, 1997, p 77-85
DSTKIM No
97-03778
CANDIS No
503970
Format(s):
Hardcopy;Document Image stored on Optical Disk

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