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

被引：56

作者：

Sebela, M

Stosová, T

Havlis, J

Wielsch, N

Thomas, H

Zdráhal, Z

Shevchenko, A

机构：

[1] Palacky Univ, Fac Sci, Dept Biochem, Olomouc, Czech Republic

[2] Masaryk Univ, Fac Sci, Dept Analyt Chem, Brno, Czech Republic

[3] Max Planck Inst Mol Cell Biol & Genet, Dresden, Germany

[4] Masaryk Univ, Fac Sci, Lab Funct Genom & Prot, Brno, Czech Republic

来源：

PROTEOMICS | 2006年 / 6卷 / 10期

关键词：

bovine trypsin; conjugate; in-gel digestion; oligosaccharicle; PMF;

D O I：

10.1002/pmic.200500576

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2959 / 2963

页数：5

共 22 条

[1] A mass spectrometric journey into protein and proteome research [J].