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Thermostable trypsin conjugates for high‐throughput proteomics: synthesis and performance evaluation
Author(s) -
Šebela Marek,
Štosová Tat'ána,
Havliš Jan,
Wielsch Natalie,
Thomas Henrik,
Zdráhal Zbyněk,
Shevchenko Andrej
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500576
Subject(s) - raffinose , trypsin , thermostability , autolysis (biology) , chemistry , biochemistry , chromatography , proteomics , enzyme , sucrose , gene
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.