Two glutaraldehyde-immobilized trypsin preparations for peptide mapping by capillary zone electrophoresis, liquid chromatography, and mass spectrometry
Two glutaraldehyde-immobilized trypsin preparations for peptide mapping by capillary zone electrophoresis, liquid chromatography, and mass spectrometry
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DOI：
10.1080/10826070801890413
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发表时间：
2008-01-01
影响因子：
1.3
通讯作者：
Waldron, Karen C.
中科院分区：
文献类型：
--
作者：
Migneault, Isabelle;Dartiguenave, Catherine;Waldron, Karen C.
Trypsin was immobilized using glutaraldehyde either by covalent attachment to aminopropyl controlled pore glass (CPG) or by direct crosslinking without a carrier. As peptide mapping is a comparative method, reproducibility of the analytical separation techniques (liquid chromatography, HPLC, and capillary zone electrophoresis, CZE) and the proteolyses resulting from both enzyme preparations were evaluated. Elution time reproducibilities of 0.3 and 0.6% were found for HPLC and CZE maps, respectively. Proteolysis reproducibility was tested for each trypsin preparation and compared with solution phase proteolysis. Sequence coverages of ca 65% were obtained from matrix-assisted laser desorption/ionization-time-of-flight (MALDI-TOF) mass spectral mapping for the two solid phase preparations.
