Transferrin presents two glycosylationsites, with the most abundant N-linked glycan ofcom position [5,4,0,2,0] at each of those two sequons
In agreementwith this, glycopeptides QQQHLFGSNVTDCSGNFCLFR-[5,4,0,2,0]and CGLVPVLAENYNK-[5,4,0,2,0] could be identified using tandemMS in both HILIC-C18 and C18 analyses
Other transferrin glycopeptides ,although identified by GlycReSoft in the C18 LC–MS data, didnot get selected for data-dependent tandem MS due to presence of abundantnonglycosylated peptides
However, these glycopeptides underwent tandemMS and could be confidently assigned in case of HILIC-C18