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Tryptic glycopeptides of IGFBP-5 from T47D cells separated by HPLC detected by ESI-MS and sequenced by tandem MS.a, ESI-MS spectrum of combined fractions.

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Presentation on theme: "Tryptic glycopeptides of IGFBP-5 from T47D cells separated by HPLC detected by ESI-MS and sequenced by tandem MS.a, ESI-MS spectrum of combined fractions."— Presentation transcript:

1 Tryptic glycopeptides of IGFBP-5 from T47D cells separated by HPLC detected by ESI-MS and sequenced by tandem MS.a, ESI-MS spectrum of combined fractions 15 and 16 containing glycopeptides. Tryptic glycopeptides of IGFBP-5 from T47D cells separated by HPLC detected by ESI-MS and sequenced by tandem MS.a, ESI-MS spectrum of combined fractions 15 and 16 containing glycopeptides. The peptide IGFBP-5-(145–156) is heterogeneously modified by O-linked glycans containing HexNAc, Hex, and NeuAc shown as square, circular, and triangular symbols, respectively. Each glycopeptide signal was sequenced (data not shown, except for the most abundant, see below), and the most likely structure was determined from the sequence information and is shown for each glycopeptide signal. b, tandem MS spectrum of the doubly charged parent at m/z 1,102.0 revealed a glycopeptide with HexNAc, Hex, and two NeuAc carbohydrates. This glycopeptide was the most abundant. Examples of the possible glycan structures and their fragmentation are shown above the spectrum in b. Mark E. Graham et al. Mol Cell Proteomics 2007;6: © 2007 The American Society for Biochemistry and Molecular Biology

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