Thermostable trypsin conjugates for high-throughput proteomics: synthesis and performance evaluation
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Fructose-Bisphosphate Aldolase chemistry MeSH
- Cytochromes c chemistry MeSH
- Gels MeSH
- Myoglobin chemistry MeSH
- Oligosaccharides chemistry MeSH
- Proteomics MeSH
- Raffinose chemistry MeSH
- Solutions MeSH
- Serum Albumin, Bovine chemistry MeSH
- Cattle MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Enzyme Stability MeSH
- Trisaccharides chemistry MeSH
- Trypsin chemistry MeSH
- Heating MeSH
- Animals MeSH
- Check Tag
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Fructose-Bisphosphate Aldolase MeSH
- Cytochromes c MeSH
- Gels MeSH
- maltotriose MeSH Browser
- Myoglobin MeSH
- Oligosaccharides MeSH
- Raffinose MeSH
- Solutions MeSH
- Serum Albumin, Bovine MeSH
- stachyose MeSH Browser
- Trisaccharides MeSH
- Trypsin MeSH
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.
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