Amine donor protein substrates for transglutaminase activity in Caenorhabditis elegans

András Mádi, Raimund Hoffrogge, Bernadett Blaskó, Michael O. Glocker, László Fésüs

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Transglutaminase dependent cross-linking of proteins has been implicated in a wide range of biological phenomena occurring in both extracellular and intracellular compartments. Clarification of the physiological role of transglutaminases requires identification of substrate molecules. Here we report the detection, purification, and identification by mass spectrometry of proteins, the glutamate dehydrogenase, a protein disulfide isomerase, and aldehyde dehydrogenase as amine donor substrates for the transglutaminase activity of the nematode Caenorhabditis elegans utilizing a novel biotinylated oligoglutamine peptide as a substrate. We also purified and identified streptavidin-binding proteins of the worm.

Original languageEnglish
Pages (from-to)1064-1069
Number of pages6
JournalBiochemical and biophysical research communications
Volume315
Issue number4
DOIs
Publication statusPublished - Mar 19 2004

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Keywords

  • Aldehyde dehydrogenase
  • Biotinylated protein
  • Glutamate dehydrogenase
  • Mass spectrometry
  • Monomeric avidin chromatography
  • Protein disulfide isomerase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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