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

Šebela, M., Štosová, T., Havliš, J., Wielsch, N., Thomas, H., Zdráhal, Z., et al. (2006). Thermostable trypsin conjugates for high-throughput proteomics: synthesis and performance evaluation. Proteomics, 6(10), 2959-2963. doi:10.1002/pmic.200500576.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-E7BF-A Version Permalink: https://hdl.handle.net/21.11116/0000-0009-3BFA-C
Genre: Journal Article

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EXT479.pdf (Publisher version), 258KB
 
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Šebela, Marek, Author
Štosová, Tat’ána, Author
Havliš, Jan, Author
Wielsch, Natalie1, Author           
Thomas, Henrik, Author
Zdráhal, Zbynĕk, Author
Shevchenko, Andrej, Author
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1External Organizations, ou_persistent22              

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 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.

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 Dates: 2006-01-092006-04-242006
 Publication Status: Issued
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 Identifiers: Other: EXT479
DOI: 10.1002/pmic.200500576
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Title: Proteomics
Source Genre: Journal
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Publ. Info: Weinheim : WILEY-VCH
Pages: - Volume / Issue: 6 (10) Sequence Number: - Start / End Page: 2959 - 2963 Identifier: ISSN: 1615-9853
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000294310