Modification-specific proteomic analysis of glycoproteins in human body fluids by mass spectrometry

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Standard

Modification-specific proteomic analysis of glycoproteins in human body fluids by mass spectrometry. / Bunkenborg, Jakob; Hägglund, Per; Jensen, Ole Norregaard.

Proteomics of Human Body Fluids: Principles, Methods, and Applications. Humana Press, 2007. p. 107-128.

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Harvard

Bunkenborg, J, Hägglund, P & Jensen, ON 2007, Modification-specific proteomic analysis of glycoproteins in human body fluids by mass spectrometry. in Proteomics of Human Body Fluids: Principles, Methods, and Applications. Humana Press, pp. 107-128. https://doi.org/10.1007/978-1-59745-432-2_5

APA

Bunkenborg, J., Hägglund, P., & Jensen, O. N. (2007). Modification-specific proteomic analysis of glycoproteins in human body fluids by mass spectrometry. In Proteomics of Human Body Fluids: Principles, Methods, and Applications (pp. 107-128). Humana Press. https://doi.org/10.1007/978-1-59745-432-2_5

Vancouver

Bunkenborg J, Hägglund P, Jensen ON. Modification-specific proteomic analysis of glycoproteins in human body fluids by mass spectrometry. In Proteomics of Human Body Fluids: Principles, Methods, and Applications. Humana Press. 2007. p. 107-128 https://doi.org/10.1007/978-1-59745-432-2_5

Author

Bunkenborg, Jakob ; Hägglund, Per ; Jensen, Ole Norregaard. / Modification-specific proteomic analysis of glycoproteins in human body fluids by mass spectrometry. Proteomics of Human Body Fluids: Principles, Methods, and Applications. Humana Press, 2007. pp. 107-128

Bibtex

@inbook{92292a54b83d40dca2bbc81b97894474,
title = "Modification-specific proteomic analysis of glycoproteins in human body fluids by mass spectrometry",
abstract = "Glycosylation of proteins is a very common, diverse, and heterogeneous type of modification, especially for proteins with extracellular destinations. This chapter describes some general strategies for the enrichment of glycoproteins and glycopeptides with an emphasis on proteomic analysis of N-glycosylated proteins in body fluids and other complex samples. An approach for identification of N-glycosylated proteins and mapping of their glycosylation sites is described. In this approach, glycoproteins are initially selectively purified by lectin chromatography. Following tryptic digestion, glycopeptides are enriched by hydrophilic interaction chromatography (HILIC). Glycan heterogeneity is then reduced by treating the glycopeptides with endoglycosidases. The resulting peptides are then analyzed by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry and nano-flow reversed-phase liquid chromatography tandem mass spectrometry (LC-MS/MS). The analysis allows the identification of N-glycosylation sites and is demonstrated on a mixture of standard proteins.",
keywords = "glycoproteomics, glycosylation, HILIC, lectin, mass spectrometry, plasma proteins, posttranslational modifications, Proteomics",
author = "Jakob Bunkenborg and Per H{\"a}gglund and Jensen, {Ole Norregaard}",
year = "2007",
month = jan,
day = "1",
doi = "10.1007/978-1-59745-432-2_5",
language = "English",
isbn = "9781588296573",
pages = "107--128",
booktitle = "Proteomics of Human Body Fluids",
publisher = "Humana Press",
address = "United States",

}

RIS

TY - CHAP

T1 - Modification-specific proteomic analysis of glycoproteins in human body fluids by mass spectrometry

AU - Bunkenborg, Jakob

AU - Hägglund, Per

AU - Jensen, Ole Norregaard

PY - 2007/1/1

Y1 - 2007/1/1

N2 - Glycosylation of proteins is a very common, diverse, and heterogeneous type of modification, especially for proteins with extracellular destinations. This chapter describes some general strategies for the enrichment of glycoproteins and glycopeptides with an emphasis on proteomic analysis of N-glycosylated proteins in body fluids and other complex samples. An approach for identification of N-glycosylated proteins and mapping of their glycosylation sites is described. In this approach, glycoproteins are initially selectively purified by lectin chromatography. Following tryptic digestion, glycopeptides are enriched by hydrophilic interaction chromatography (HILIC). Glycan heterogeneity is then reduced by treating the glycopeptides with endoglycosidases. The resulting peptides are then analyzed by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry and nano-flow reversed-phase liquid chromatography tandem mass spectrometry (LC-MS/MS). The analysis allows the identification of N-glycosylation sites and is demonstrated on a mixture of standard proteins.

AB - Glycosylation of proteins is a very common, diverse, and heterogeneous type of modification, especially for proteins with extracellular destinations. This chapter describes some general strategies for the enrichment of glycoproteins and glycopeptides with an emphasis on proteomic analysis of N-glycosylated proteins in body fluids and other complex samples. An approach for identification of N-glycosylated proteins and mapping of their glycosylation sites is described. In this approach, glycoproteins are initially selectively purified by lectin chromatography. Following tryptic digestion, glycopeptides are enriched by hydrophilic interaction chromatography (HILIC). Glycan heterogeneity is then reduced by treating the glycopeptides with endoglycosidases. The resulting peptides are then analyzed by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry and nano-flow reversed-phase liquid chromatography tandem mass spectrometry (LC-MS/MS). The analysis allows the identification of N-glycosylation sites and is demonstrated on a mixture of standard proteins.

KW - glycoproteomics

KW - glycosylation

KW - HILIC

KW - lectin

KW - mass spectrometry

KW - plasma proteins

KW - posttranslational modifications

KW - Proteomics

UR - http://www.scopus.com/inward/record.url?scp=84857118081&partnerID=8YFLogxK

U2 - 10.1007/978-1-59745-432-2_5

DO - 10.1007/978-1-59745-432-2_5

M3 - Book chapter

AN - SCOPUS:84857118081

SN - 9781588296573

SP - 107

EP - 128

BT - Proteomics of Human Body Fluids

PB - Humana Press

ER -

ID: 240160977