Abstract
The FAB-mass spectrometric fragmentation behavior of two dynorphins (heptapeptide, tridecapeptide) were studied in a four-sector (B 1E 1E 2B 2) mass spectrometer. The (M+H) + ion is selected by the first two fields (B 1, E 1) and product ions arising from either unimolecular or collision-activated dissociation are collected by a linked-field (B 2/E 2) scan of the second two fields. Important product-precursor relationships required for peptide identification and eventual quantification are established because fragment ions found in the B 2/E 2 scan derive only from the (M+H) + ion of the peptide. For the heptapeptide, more C-terminus containing ions were found in the B 2/E 2 linked-field scan data, whereas for the tridecapeptide, abundant ions containing the N- and C-termini were found.
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