作者: Thorsten W. Jaskolla , Dimitrios G. Papasotiriou , Michael Karas
DOI: 10.1021/PR900274S
关键词: Pepsin 、 Chymotrypsin 、 alpha-Cyano-4-hydroxycinnamic acid 、 Peptide 、 Chromatography 、 Chemistry 、 Protein mass spectrometry 、 Protease 、 Isoelectric point 、 Trypsin
摘要: The performance of the recently developed 4-chloro-α-cyanocinnamic acid (Cl-CCA) matrix-assisted laser desorption ionization mass spectrometry (MALDI MS) matrix was investigated in comparison to most widely used α-cyano-4-hydroxycinnamic (CHCA). For this purpose, in-solution digestions standard proteins low femtomole range with proteases trypsin, chymotrypsin, and pepsin were as analytes. all protein−protease combinations, Cl-CCA revealed be highly superior terms number identified peptides, obtained sequence coverages peptide detection reproducibility. A deeper inspection detected signals regard both physicochemical properties (their isoelectric point) spectrometric (signal-to-noise ratios accuracies) showed that progress achieved is due numerous acidic neutral peptides. Moreover, higher sensitivity allowed for addit...