Modification of Trypsin for Improvement of Its Stability in Protein Digestion Process
| Authors | |
|---|---|
| Year of publication | 2006 |
| Type | Conference abstract |
| MU Faculty or unit | |
| 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: |