Mádi András, Hoffrogge Raimund, Blaskó Bernadett, Glocker Michael O, Fésüs László
Signalling and Apoptosis Research Group of the Hungarian Academy of Sciences, University of Debrecen, Debrecen, Hungary.
Biochem Biophys Res Commun. 2004 Mar 19;315(4):1064-9. doi: 10.1016/j.bbrc.2004.01.159.
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.
