title: Permethylated N-glycan analysis with mass spectrometry.
abstract: Protein glycosylation plays an important role in multiple cell functions, and aberrations of protein glycosylation are associated with various malignancies including cancer. In this chapter, we provide a detailed protocol for MALDI MS analysis of permethylated N-glycans extracted from human serum proteins. The protocol includes procedures for N-glycan purification and in-solution permethylation, structural elucidation of permethylated N-glycans by MALDI-QIT-TOF MS, and construction of indices to quantify levels of certain types of glycosylation, such as fucosylation, which may serve as a potential disease biomarker.
authors.affiliation: Department of Chemistry, University of Michigan, Ann Arbor, MI, USA.
authors.forename: Zhenxin
authors.initials: Z
authors.lastname: Lin
authors.forename: David M
authors.initials: DM
authors.lastname: Lubman
mesh_terms: D014408:Biomarkers, Tumor / Q000032:analysis; D001798:Blood Proteins / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry*; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods*; D009369:Neoplasms / Q000378:metabolism; D011134:Polysaccharides / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D000093422:Glycated Serum Proteins
chemical_list: D014408:Biomarkers, Tumor; D001798:Blood Proteins; D006023:Glycoproteins; D011134:Polysaccharides; D000093422:Glycated Serum Proteins