Modification of Trypsin for Improvement of Its Stability in Protein Digestion Process

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Authors	HAVLIŠ Jan ŠEBELA Marek ŠTOSOVÁ Tatiana TARKOWSKI Petr WIELSCH Natalie THOMAS Henrik SHEVCHENKO Andrej
Year of publication	2006
Type	Conference abstract
MU Faculty or unit	Faculty of Science
Citation
Description	A typical MS-assisted proteomic routine involves protease trypsin to generate specific fragments for further analysis. As the enzyme shows marginal termostability and undegoes intense autolysis, it became important to improve its properties in this regard. Conjugation of trypsin with e.g. oligosaccharides (maltotriose, raffinose, stachyose) is one the possible ways to solve these problems. Another way might be use of proteases of similar specifity from bacteria. Both approches were tested and particular proteases were characterised by means of their biochemical (pI, mol.mass, kinetics) and MS-related properties (cleavage efficiency).
Related projects:	Proteins in metabolism and interaction of organisms with the environment