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PXD004289

PXD004289 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleSite-specific glycosylation of donkey milk lactoferrin investigated by High Resolution Mass Spectrometry
DescriptionA comprehensive glycosylation profile of donkey lactoferrin, isolated by ion exchange chromatography from an individual milk sample, was obtained by means of chymotryptic digestion, TiO2 and HILIC enrichment, reversed-phase high performance liquid chromatography, electrospray mass spectrometry, and high collision dissociation fragmentation. The results obtained allowed the identification of 26 different glycan structures, including high mannose, complex and hybrid N-glycans, linked to the protein backbone via an amide bond to asparagine residues located at the positions 137, 281 and 476. Altogether, the N-glycan structures determined revealed that in donkey milk lactoferrin most of the N-glycans identified are neutral complex/hybrid. Actually, 10 neutral non-fucosylated complex/hybrid N-glycans and 4 neutral fucosylated complex/hybrid N-glycans were found. In addition, 2 high mannose N-glycans, 4 sialylated fucosylated complex/hybrid N-glycans and 6 sialylated non-fucosylatedN-glycans, one of which containing N-glycolylneuramin acid (Neu5Gc), were found. A comparison of the glycosylation profile of donkey milk lactoferrin with respect to that of human, bovine and goat milk lactoferrin is reported.
HostingRepositoryPRIDE
AnnounceDate2016-08-25
AnnouncementXMLSubmission_2016-08-25_00:41:21.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterSalvatore Foti
SpeciesList scientific name: Equus asinus (Donkey); NCBI TaxID: 9793;
ModificationListcomplex glycosylation
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02016-06-08 04:04:32ID requested
12016-08-25 00:41:22announced
Publication List
Gallina S, Saletti R, Cunsolo V, Muccilli V, Foti S, Roepstorff P, Rasmussen MI, Site-specific glycosylation of donkey milk lactoferrin investigated by high-resolution mass spectrometry. Amino Acids, 48(12):2799-2808(2016) [pubmed]
Keyword List
curator keyword: Biological
submitter keyword: Lactoferrin glycosylation · Donkey milk · N-glycan structures · TiO2 and HILIC enrichment · Mass spectrometry
Contact List
Salvatore Foti
contact affiliationOrganic Mass Spectrometry Laboratory, Department of Chemical Sciences, University of Catania, Viale A. Doria 6, I-95125 Catania, Italy
contact emailsfoti@unict.it
lab head
Salvatore Foti
contact affiliationUniversity of Catania
contact emailsfoti@unict.it
dataset submitter
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Dataset FTP location
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