An electrophoretic approach to screen for glutamine deamidation

Anal Biochem. 2012 Sep 1;428(1):1-3. doi: 10.1016/j.ab.2012.05.016. Epub 2012 May 26.

Abstract

Protein deamidation is a posttranslational modification with important implications in physiology and medicine. There is, however, no simple technique for a rapid screening of protein deamidation. The deamidating activity of transglutaminase was applied to establish a simple method for the screen of protein deamidation using recombinant human growth hormone, a rat hippocampal membrane fraction, and a cell homogenate enriched in 5-hydroxytryptamine-1A receptor as model systems. Here we report a simple, economic, and fast approach to assess protein deamidation by two electrophoretic methods: differential cleavage on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) via in situ V8 protease digestion and the principle of spot shifting via blue native (BN)-PAGE/two-dimensional (2D)-SDS-PAGE/immunoblotting.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amides / metabolism*
  • Animals
  • Buffers
  • Cell Extracts
  • Electrophoresis, Gel, Two-Dimensional / methods*
  • Glutamine / analysis*
  • Human Growth Hormone / metabolism
  • Humans
  • Membranes / metabolism
  • Rats
  • Receptor, Serotonin, 5-HT1A / metabolism
  • Staining and Labeling
  • Subcellular Fractions / metabolism

Substances

  • Amides
  • Buffers
  • Cell Extracts
  • Glutamine
  • Receptor, Serotonin, 5-HT1A
  • Human Growth Hormone