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@proceedings{695994, author = {Havliš, Jan and Šebela, Marek and Štosová, Tatiana and Tarkowski, Petr and Wielsch, Natalie and Thomas, Henrik and Shevchenko, Andrej}, booktitle = {Abstract Book 17th IMSC Prague}, keywords = {trypsin; tryptic digestion; PMF; modified trypsin}, language = {eng}, title = {Modification of Trypsin for Improvement of Its Stability in Protein Digestion Process}, year = {2006} }
TY - CONF ID - 695994 AU - Havliš, Jan - Šebela, Marek - Štosová, Tatiana - Tarkowski, Petr - Wielsch, Natalie - Thomas, Henrik - Shevchenko, Andrej PY - 2006 TI - Modification of Trypsin for Improvement of Its Stability in Protein Digestion Process KW - trypsin KW - tryptic digestion KW - PMF KW - modified trypsin N2 - 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). ER -
HAVLIŠ, Jan, Marek ŠEBELA, Tatiana ŠTOSOVÁ, Petr TARKOWSKI, Natalie WIELSCH, Henrik THOMAS and Andrej SHEVCHENKO. Modification of Trypsin for Improvement of Its Stability in Protein Digestion Process. In \textit{Abstract Book 17th IMSC Prague}. 2006.
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