Abstract
Human α1-microglobulin (α1-m; also called protein HC), a glycoprotein belonging to the lipocalin superfamily, was isolated by sequential anion-exchange chromatography and gel filtration from the urine of hemodialized patients and from amniotic fluid collected in the week 16-18 of pregnancy. The carbohydrate chains of the protein purified from the two sources, which are organized in two Asn-linked and one Thr-linked oligosaccharides, were structurally characterized using matrix-assisted laser desorption ionization and electrospray mass spectrometry. The glycans attached to Thr5 are differently truncated NeuHexHexNAc sequences, and O- glycosylation in the amniotic fluid protein is only partial. Asn96 has both diantennary and triantennary structures attached in the case of urinary α1- m and only diantennary glycans in the amniotic fluid protein. The main carbohydrate units attached to Asn17 are in both proteins monosialylated and disialylated diantennary glycans. The position of the oligosaccharide chains in a three-dimensional model of the protein, produced using the automated Swiss-Model service, is also discussed.
| Original language | English |
|---|---|
| Pages (from-to) | 2105-2112 |
| Number of pages | 8 |
| Journal | European Journal of Biochemistry |
| Volume | 267 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - 2000 |
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Keywords
- α-microglobulin
- Lipocalins
- Mass spectrometry
- Oligosaccharide structure
ASJC Scopus subject areas
- Biochemistry
Cite this
Structural characterization of the oligosaccharide chains of human α1- microglobulin from urine and amniotic fluid. / Amoresano, Angela; Minchiotti, Lorenzo; Cosulich, Maria E.; Campagnoli, Monica; Pucci, Piero; Andolfo, Annapaola; Gianazza, Elisabetta; Galliano, Monica.
In: European Journal of Biochemistry, Vol. 267, No. 7, 2000, p. 2105-2112.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structural characterization of the oligosaccharide chains of human α1- microglobulin from urine and amniotic fluid
AU - Amoresano, Angela
AU - Minchiotti, Lorenzo
AU - Cosulich, Maria E.
AU - Campagnoli, Monica
AU - Pucci, Piero
AU - Andolfo, Annapaola
AU - Gianazza, Elisabetta
AU - Galliano, Monica
PY - 2000
Y1 - 2000
N2 - Human α1-microglobulin (α1-m; also called protein HC), a glycoprotein belonging to the lipocalin superfamily, was isolated by sequential anion-exchange chromatography and gel filtration from the urine of hemodialized patients and from amniotic fluid collected in the week 16-18 of pregnancy. The carbohydrate chains of the protein purified from the two sources, which are organized in two Asn-linked and one Thr-linked oligosaccharides, were structurally characterized using matrix-assisted laser desorption ionization and electrospray mass spectrometry. The glycans attached to Thr5 are differently truncated NeuHexHexNAc sequences, and O- glycosylation in the amniotic fluid protein is only partial. Asn96 has both diantennary and triantennary structures attached in the case of urinary α1- m and only diantennary glycans in the amniotic fluid protein. The main carbohydrate units attached to Asn17 are in both proteins monosialylated and disialylated diantennary glycans. The position of the oligosaccharide chains in a three-dimensional model of the protein, produced using the automated Swiss-Model service, is also discussed.
AB - Human α1-microglobulin (α1-m; also called protein HC), a glycoprotein belonging to the lipocalin superfamily, was isolated by sequential anion-exchange chromatography and gel filtration from the urine of hemodialized patients and from amniotic fluid collected in the week 16-18 of pregnancy. The carbohydrate chains of the protein purified from the two sources, which are organized in two Asn-linked and one Thr-linked oligosaccharides, were structurally characterized using matrix-assisted laser desorption ionization and electrospray mass spectrometry. The glycans attached to Thr5 are differently truncated NeuHexHexNAc sequences, and O- glycosylation in the amniotic fluid protein is only partial. Asn96 has both diantennary and triantennary structures attached in the case of urinary α1- m and only diantennary glycans in the amniotic fluid protein. The main carbohydrate units attached to Asn17 are in both proteins monosialylated and disialylated diantennary glycans. The position of the oligosaccharide chains in a three-dimensional model of the protein, produced using the automated Swiss-Model service, is also discussed.
KW - α-microglobulin
KW - Lipocalins
KW - Mass spectrometry
KW - Oligosaccharide structure
UR - http://www.scopus.com/inward/record.url?scp=0034037464&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034037464&partnerID=8YFLogxK
U2 - 10.1046/j.1432-1327.2000.01217.x
DO - 10.1046/j.1432-1327.2000.01217.x
M3 - Article
C2 - 10727951
AN - SCOPUS:0034037464
VL - 267
SP - 2105
EP - 2112
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
SN - 0014-2956
IS - 7
ER -