TY - JOUR
T1 - N- and O-linked glycosylation site profiling of the human basic salivary proline-rich protein 3M.
AU - Manconi, Barbara
AU - Cabras, Tiziana
AU - Sanna, Maria Teresa
AU - Piras, V
AU - Liori, B
AU - Pisano, Elisabetta
AU - Iavarone, Federica
AU - Vincenzoni, Federica
AU - Cordaro, Massimo
AU - Faa, G
AU - Castagnola, Massimo
AU - Messana, Irene
PY - 2016
Y1 - 2016
N2 - In the present study, we show that the heterogeneous mixture of glycoforms of the basic salivary proline-rich protein 3M, encoded by PRB3-M locus, is a major component of the acidic soluble fraction of human whole saliva in the first years of life. Reversed-phase high-performance liquid chromatography with high-resolution electrospray ionization mass spectrometry analysis of the intact proteoforms before and after N-deglycosylation with Peptide-N-Glycosidase F and tandem mass spectrometry sequencing of peptides obtained after Endoproteinase GluC digestion allowed the structural characterization of the peptide backbone and identification of N- and O-glycosylation sites. The heterogeneous mixture of the proteoforms derives from the combination of 8 different neutral and sialylated glycans O-linked to Threonine 50, and 33 different glycans N-linked to Asparagine residues at positions 66, 87, 108, 129, 150, 171, 192, and 213.
AB - In the present study, we show that the heterogeneous mixture of glycoforms of the basic salivary proline-rich protein 3M, encoded by PRB3-M locus, is a major component of the acidic soluble fraction of human whole saliva in the first years of life. Reversed-phase high-performance liquid chromatography with high-resolution electrospray ionization mass spectrometry analysis of the intact proteoforms before and after N-deglycosylation with Peptide-N-Glycosidase F and tandem mass spectrometry sequencing of peptides obtained after Endoproteinase GluC digestion allowed the structural characterization of the peptide backbone and identification of N- and O-glycosylation sites. The heterogeneous mixture of the proteoforms derives from the combination of 8 different neutral and sialylated glycans O-linked to Threonine 50, and 33 different glycans N-linked to Asparagine residues at positions 66, 87, 108, 129, 150, 171, 192, and 213.
KW - Protein
KW - Protein
UR - https://publicatt.unicatt.it/handle/10807/96013
UR - https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=84992301023&origin=inward
UR - https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84992301023&origin=inward
U2 - 10.1002/jssc.201501306
DO - 10.1002/jssc.201501306
M3 - Article
SN - 1615-9306
VL - 39
SP - 1987
EP - 1997
JO - Journal of Separation Science
JF - Journal of Separation Science
IS - 10
ER -