Journal
AMINO ACIDS
Volume 48, Issue 7, Pages 1569-1580Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-016-2209-0
Keywords
Lactoferrin; Sequence characterization; Glycosylation sites; Donkey milk; Mass spectrometry
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Funding
- POR project BRIT [CUP E61D11000280007]
- [PO FERS 2007/13 4.1.2.A]
- [CUP B65E12000570008]
- Villum Fonden [00007292] Funding Source: researchfish
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Lactoferrin, a protein showing an array of biochemical properties, including immuno-modulation, iron-binding ability, as well as antioxidant, antibacterial and antiviral activities, but which may also represent a potential milk allergen, was isolated from donkey milk by ion exchange chromatography. The characterization of its primary structure, by means of enzymatic digestions, SPITC derivatization of tryptic digest, reversed-phase high performance liquid chromatography, electrospray and matrix-assisted laser desorption/ionization mass spectrometry, is reported. Our results allowed the almost complete characterization of donkey lactoferrin sequence, that, at least for the covered sequence, differs from the horse genomic deduced sequence (UniProtKB Acc. Nr. O77811) by five point substitutions located at positions 91 (Arg -> His), 328 (Thr -> Ile/Leu), 466 (Ala -> Gly), 642 (Asn -> Ser) and 668 (Ser -> Ala). Analysis of the glycosylated protein showed that glycans in donkey lactoferrin are linked to the protein backbone via an amide bond to asparagine residues located at the positions 137, 281 and 476.
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