title: Mass spectrometric analysis of mucin core proteins.
abstract: Mucins are difficult to handle for their identification and characterization via proteomic applications due to their heavily glycosylated nature (up to 90%), high molecular weight (200 kDa-200 MDa), and size (Rg 10-300 nm). Their core proteins are extremely large and highly substituted with oligosaccharides, which only allow access to a highly restricted portion of their protein. For this reason, conventional 1D or 2D polyacrylamide gel-based proteomic approaches are not effective for identification and characterization of mucin molecules. In this chapter, we present our current protocol employing a modified shotgun proteomic approach to identify these complex glycoproteins.
authors.affiliation: Department of Biochemistry and Biophysics Cystic Fibrosis/Pulmonary Research Center, University of North Carolina, 4021 Thurston Bowles Bldg. CB#7248, Chapel Hill, NC, USA. kesimer@med.unc.edu
authors.forename: Mehmet
authors.initials: M
authors.lastname: Kesimer
authors.forename: John K
authors.initials: JK
authors.lastname: Sheehan
mesh_terms: D006801:Humans; D013058:Mass Spectrometry; D008970:Molecular Weight; D009077:Mucins / Q000032:analysis* / Q000737:chemistry*; D010316:Particle Size; D040901:Proteomics
chemical_list: D009077:Mucins