期刊
JOURNAL OF CHROMATOGRAPHY A
卷 1217, 期 51, 页码 8032-8040出版社
ELSEVIER
DOI: 10.1016/j.chroma.2010.08.058
关键词
IMAC phosphopeptide separation; IDA-modified magnetic microspheres; Porcine pepsin A; Bovine alpha-casein; Bovine milk
Magnetic non-porous hydrophilic poly(2-hydroxyethyl methacrylate-co-glycidyl methacrylate) microspheres prepared by the dispersion polymerization and modified with iminodiacetic acid (IDA) were employed for the IMAC separation of phosphopeptides. Fe3+ and Ga3+ ions immobilized on IDA-modified magnetic microspheres were used for the enrichment of phosphopeptides from the proteolytic digests of two model proteins differing in their physico-chemical properties and phosphate group content: porcine pepsin A and bovine a-casein. The optimum conditions for phosphopeptide adsorption and desorption in both cases were investigated and compared. The phosphopeptides separated from the proteolytic digests were analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The ability of the prepared Fe3+- and Ga3+-IDA-modified magnetic microspheres to capture phosphopeptides from complex mixtures was shown on an example of bovine milk proteolytic digest. (C) 2010 Elsevier B.V. All rights reserved.
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