English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons219229

Havlis,  Jan
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons16217

Wielsch,  Natalie
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons219733

Thomas,  Henrik
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons218972

Shevchenko,  Andrej
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Sebela, M., Stosova, T., Havlis, J., Wielsch, N., Thomas, H., Zdrahal, Z., et al. (2006). Thermostable trypsin conjugates for high-throughput proteomics: synthesis and performance evaluation. PROTEOMICS, 6(10), 2959-2963.


Cite as: https://hdl.handle.net/21.11116/0000-0001-10C4-F
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.