4.8 Article

Glycomic Analysis Using Glycoprotein Immobilization for Glycan Extraction

期刊

ANALYTICAL CHEMISTRY
卷 85, 期 11, 页码 5555-5561

出版社

AMER CHEMICAL SOC
DOI: 10.1021/ac400761e

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资金

  1. National Institutes of Health, National Cancer Institute
  2. Early Detection Research Network (EDRN) [U01CA152813]
  3. Clinical Proteomic Tumor Analysis Consortium (CPTAC) [U24CA160036]
  4. National Institutes of Health, National Heart Lung and Blood Institute Programs of Excellence in Glycosicences(PEG) [P01HL107153]
  5. Johns Hopkins Proteomics Center [N01-HV-00240]

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Glycosylation is one of the most common protein modifications and is involved in many functions of glycoproteins. Investigating aberrant protein glycosylation associated with diseases. is useful in improving disease diagnostics. Due to the nontemplate nature of glycan biosynthesis, the glycans attached to glycoproteins are enormously complex; thus, a method for comprehensive analysis of glycans from biological or clinical samples needed. ere, e describe a novel method for glyco analysis using glyoprotein immobilization for glycan extraction (GIG). Proteins or peptides from complex samples were first immobilized on solid support, and other nonconjugated molecules were removed. Glycans were enzymatically or chemically modified on solid phase before releasing from glycoproteins/glycopeptides for mass spectrometry analysis. method was applied to the glycomic analysis of both N- and O-glycans.

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