Post-translational modifications on proteins: Facile and efficient procedure for the identification of O-glycosylation sites by MALDI-LIFT-TOF/TOF mass spectrometry
被引:31
作者:
Kurogochi, M
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机构:
Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Frontier Res Ctr Post Gen Sci & Technol, Sapporo, Hokkaido 0010021, JapanHokkaido Univ, Grad Sch Sci, Div Biol Sci, Frontier Res Ctr Post Gen Sci & Technol, Sapporo, Hokkaido 0010021, Japan
Kurogochi, M
[1
]
Matsushita, T
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机构:
Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Frontier Res Ctr Post Gen Sci & Technol, Sapporo, Hokkaido 0010021, JapanHokkaido Univ, Grad Sch Sci, Div Biol Sci, Frontier Res Ctr Post Gen Sci & Technol, Sapporo, Hokkaido 0010021, Japan
Matsushita, T
[1
]
Nishimura, SI
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Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Frontier Res Ctr Post Gen Sci & Technol, Sapporo, Hokkaido 0010021, JapanHokkaido Univ, Grad Sch Sci, Div Biol Sci, Frontier Res Ctr Post Gen Sci & Technol, Sapporo, Hokkaido 0010021, Japan
Nishimura, SI
[1
]
机构:
[1] Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Frontier Res Ctr Post Gen Sci & Technol, Sapporo, Hokkaido 0010021, Japan
glycosylation;
high-throughput screening;
mass spectrometry;
protein modifications;
proteomics;
D O I:
10.1002/anie.200460020
中图分类号:
O6 [化学];
学科分类号:
0703 ;
摘要:
We have LIFT-TOF! Transglycosylation of glycopeptides by β-galactosidase in the presence of lactose combined with tandem mass spectrometry using a 2,5-dihydroxybenzoic acid matrix enables the O-glycosylation sites to be identified (see scheme). The highly sensitive and ideal fragmentation patterns generated from glycopeptide precursor ion peaks can be readily used for precise and reliable structure analyses.