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Cited by 405

The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.

Human Plasma N-Glycoproteome Analysis by Immunoaffinity Subtraction, Hydrazide Chemistry, and Mass Spectrometry

Open access
Liu, Tao, Qian, Wei-Jun, Gritsenko, Marina A., Camp, David G., Monroe, Matthew E., Moore, Ronald J., Smith, Richard D.·2005·Journal of Proteome Research
DOI 10.1021/pr0502065
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Abstract

The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies. Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity. Six high-abundance plasma proteins were simultaneously removed using a pre-packed, immobilized antibody column. N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F). Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS). Using stringent criteria, a total of 2053 different N-glycopeptides were confidently identified, covering 303 nonredundant N-glycoproteins. This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL). A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.

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Metadata

Authors
Liu, T., Qian, W.-J., Gritsenko, M. A., Camp, D. G., Monroe, M. E., Moore, R. J., & Smith, R. D.
Venue
Journal of Proteome Research
Publisher
American Chemical Society (ACS)
Published
2005-10-26
Volume
4
Issue
6
Pages
2070-2080
ISSN
  • 1535-3893 (ISSN-L)
  • 1535-3907
DOI
10.1021/pr0502065
OpenAlex
W1971280282
Cited by
405
References
42
FWCI
7.95
Type
journal article
Language
en
Open access
green

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