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Measurement of initial translational energies of peptide ions in laser desorption/ionization mass spectrometry
Author(s) -
Pan Ying,
Cotter Robert J.
Publication year - 1992
Publication title -
organic mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0030-493X
DOI - 10.1002/oms.1210270103
Subject(s) - mass spectrometry , ion , kinetic energy , chemistry , ionization , soft laser desorption , desorption , reflectron , ion source , time of flight mass spectrometry , matrix assisted laser desorption/ionization , analytical chemistry (journal) , atomic physics , chromatography , physics , organic chemistry , quantum mechanics , adsorption
The initial kinetic energy distribution of [Arg]‐vasopressin molecular ions generated by matrix‐assisted UV laser desorption/ionization was measured using a delayed ion extraction, linear time‐of‐flight mass spectrometer. Energy distributions of the nicotinic acid matrix ions, with or without the presence of peptide, were also measured. These were compared with the kinetic energy distribution of gramicidin‐S ions using IR laser desorption. The measured molecular ion kinetic energy distribution from vasopressin is much broader than that from gramicidin‐S, and is characterized by a high‐energy tail that most likely results from entrainment of anlayte ions in the higher velocity matrix ions and fragments as they leave the surface.