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Fragmentation characteristics of neuropeptides related to chromogranin B and proenkephalin B using fast atom bombardment and collision‐induced dissociation
Author(s) -
Boel S.,
Dillen L.,
van den Heuvel H.,
Claeys M.
Publication year - 1994
Publication title -
biological mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1052-9306
DOI - 10.1002/bms.1200231002
Subject(s) - fragmentation (computing) , chemistry , fast atom bombardment , ion , collision induced dissociation , chromogranin a , dissociation (chemistry) , mass spectrum , proenkephalin , tandem mass spectrometry , mass spectrometry , amino acid , biochemistry , chromatography , enkephalin , biology , organic chemistry , ecology , immunohistochemistry , immunology , receptor , opioid
This study deals with the mass spectral characterization of selected neuropeptides related to chromogranin B and proenkephalin B precursor proteins using fast atom bombardment (FAB) ionization in combination with low‐ and high‐energy collision‐induced dissociation. Fragmentation pathways were investigated using linked scan and tandem mass spectrometric techniques. First‐order FAB mass spectra and product ion spectra of [M + H] + ions are discussed and analysed for structure‐specific information. In the high‐energy production spectra, abundant y and c ions are found to be indicative of the presence of proline and threonine residues, respectively. With regard to side chain specific ions, diagnostic d and w ions are found, which support the presence of leucine, glutamic acid and glutamine at specific positions in the amino acid sequence.