Thermostable trypsin conjugates for high-throughput proteomics: synthesis and performance evaluation
Related Experiment Video
Updated: Aug 9, 2026
12:07
Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
Marek Sebela1, Tat'ána Stosová, Jan Havlis
1Department of Biochemistry, Faculty of Science, Palacký University, Slechtitelů 11, 783 71 Olomouc, Czech Republic. sebela@prfholnt.upol.cz
Proteomics
|April 26, 2006
Abstract:
Conjugating bovine trypsin with oligosaccharides maltotriose, raffinose and stachyose increased its thermostability and suppressed autolysis, without affecting its cleavage specificity. These conjugates accelerated the digestion of protein substrates both in solution and in gel, compared to commonly used unmodified and methylated trypsins.
