Thermostable trypsin conjugates for high-throughput proteomics: synthesis and 
performance evaluation

Šebela, Marek; Štosová, Tat’ána; Havliš, Jan; Wielsch, Natalie; Thomas, Henrik; Zdráhal, Zbynĕk; Shevchenko, Andrej

doi:10.1002/pmic.200500576

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Thermostable trypsin conjugates for high-throughput proteomics: synthesis and performance evaluation

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Šebela, M., Štosová, T., Havliš, J., Wielsch, N., Thomas, H., Zdráhal, Z., et al. (2006). Thermostable trypsin conjugates for high-throughput proteomics: synthesis and performance evaluation. Proteomics, 6(10), 2959-2963. doi:10.1002/pmic.200500576.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-E7BF-A

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.