| Literature DB >> 14528495 |
Yingda Xu1, Merlin L Bruening, J Throck Watson.
Abstract
High concentrations of contaminants such as salts and surfactants are often present in biological samples to solubilize or stabilize analytes such as proteins. Unfortunately, the presence of those contaminants often precludes direct analysis by MALDI-MS. Selective adsorption of analytes directly on modified MALDI probes, followed by rinsing to remove contaminants, overcomes this problem. This review focuses on various modifications of MALDI probes to allow the adsorption of proteins and DNA, even in a large excess of salt or surfactant. Interfaces deposited on the MALDI probes to adsorb analytes include films of commercial polymers, thin layers of matrix crystals, self-assembled monolayers, and ultrathin polymer films. Hydrophobic and ionic interactions both effect analyte adsorption on those interfaces, and patterned interfaces allow the concentration and purification of analyte molecules. Copyright 2003 Wiley Periodicals, Inc., Mass Spec Rev 22:429-440, 2003; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/mas.10064Entities:
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Year: 2003 PMID: 14528495 DOI: 10.1002/mas.10064
Source DB: PubMed Journal: Mass Spectrom Rev ISSN: 0277-7037 Impact factor: 10.946