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 Abstract Book 17th IMSC Prague. 2006.
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Basic information
Original name Modification of Trypsin for Improvement of Its Stability in Protein Digestion Process
Name in Czech Modifikace trypsinu pro zlepšení stability v procesu štěpení proteinů
Authors HAVLIŠ, Jan (203 Czech Republic, guarantor), Marek ŠEBELA (203 Czech Republic), Tatiana ŠTOSOVÁ (203 Czech Republic), Petr TARKOWSKI (203 Czech Republic), Natalie WIELSCH (276 Germany), Henrik THOMAS (276 Germany) and Andrej SHEVCHENKO (643 Russian Federation).
Edition Abstract Book 17th IMSC Prague, 2006.
Other information
Original language English
Type of outcome Conference abstract
Field of Study 10600 1.6 Biological sciences
Country of publisher Czech Republic
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14310/06:00017201
Organization unit Faculty of Science
Keywords in English trypsin; tryptic digestion; PMF; modified trypsin
Tags modified trypsin, PMF, Trypsin, tryptic digestion
Tags International impact
Changed by Changed by: doc. Mgr. Jan Havliš, Dr., učo 743. Changed: 9/4/2010 13:37.
Abstract
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).
Abstract (in Czech)
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).
Links
MSM0021622413, plan (intention)Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
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