Detection of O-GlcNAc modifications on cardiac myofilament proteins

Methods Mol Biol. 2013:1005:157-68. doi: 10.1007/978-1-62703-386-2_13.

Abstract

In this chapter it is described a general method that has been used successfully by more than one laboratory interested in detecting O-GlcNAc in myofilament proteins. Alternative reagents for chemo-enzymatic or metabolic labeling will be indicated, as well as references for more details in alternative methods. The outline is divided into (1) Enrichment of O-GlcNAc Stoichiometry, (2) Cardiac Myofilament Protein Isolation, (3) SDS-PAGE, (4) "Reduction and Alkylation," (5) In-Gel Protein Digestion, (6) Chemo-enzymatic Labeling of O-GlcNAc Moieties (Click Chemistry), (7) Biotin Alkyne Tagging, (8) Strong Cation Exchange (SCX) and Streptavidin, and (9) β-Elimination and Michael Addition (BEMAD) for O-GlcNAc Site-Mapping.

MeSH terms

  • Acetylglucosamine / chemistry
  • Acetylglucosamine / metabolism*
  • Animals
  • Biotin
  • Click Chemistry
  • Electrophoresis, Polyacrylamide Gel
  • Glycosylation
  • Mass Spectrometry
  • Mice
  • Myocardium / chemistry*
  • Myocardium / metabolism
  • Myofibrils / chemistry*
  • Myofibrils / metabolism
  • Peptide Mapping
  • Proteins / chemistry*
  • Proteins / metabolism
  • Rats
  • Staining and Labeling / methods*
  • Streptavidin
  • beta-N-Acetylhexosaminidases / antagonists & inhibitors
  • beta-N-Acetylhexosaminidases / metabolism

Substances

  • Proteins
  • Biotin
  • Streptavidin
  • hexosaminidase C
  • beta-N-Acetylhexosaminidases
  • Acetylglucosamine