Thermostable trypsin conjugates for high-throughput proteomics: synthesis and performance evaluation.
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.
Sebela
Marek
M
Department of Biochemistry, Faculty of Science, Palacký University, Slechtitelů 11, 783 71 Olomouc, Czech Republic. sebela@prfholnt.upol.cz
Stosová
Tat'ána
T
Havlis
Jan
J
Wielsch
Natalie
N
Thomas
Henrik
H
Zdráhal
Zbynek
Z
Shevchenko
Andrej
A
D000818:Animals; D002417:Cattle; D045304:Cytochromes c / Q000737:chemistry; D004795:Enzyme Stability; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry; D005782:Gels; D006361:Heating; D009211:Myoglobin / Q000737:chemistry; D009844:Oligosaccharides / Q000737:chemistry; D040901:Proteomics; D011887:Raffinose / Q000737:chemistry; D012710:Serum Albumin, Bovine / Q000737:chemistry; D012996:Solutions; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014312:Trisaccharides / Q000737:chemistry; D014357:Trypsin / Q000737:chemistry*
D005782:Gels; D009211:Myoglobin; D009844:Oligosaccharides; D012996:Solutions; D014312:Trisaccharides; C005695:stachyose; D012710:Serum Albumin, Bovine; C008317:maltotriose; D045304:Cytochromes c; D014357:Trypsin; D005634:Fructose-Bisphosphate Aldolase; D011887:Raffinose