| Literature DB >> 16414315 |
Dmitri Sitnikov1, Donovan Chan, Eric Thibaudeau, Marc Pinard, Joanna M Hunter.
Abstract
Removal of high abundance proteins is widely used in sample processing for proteomics studies of blood plasma. Immunoaffinity (IA) depletion is currently the most specific method for performing this step. Historically, IA depletion matrices have been designed to be used with inorganic buffers. However, the presence of salts in depleted samples presents a particular problem, and these must be removed in order to make samples compatible with post-depletion processing. Desalting (dialysis, ultrafiltration, size-exclusion, etc.) usually diminishes sample integrity due to labware associated losses. Moreover, these steps require additional labor, increasing the processing time and cost of analysis. In order to avoid these problems, we have developed an IA method using a volatile buffer that can be removed from depleted samples by lyophilization. This method allows the execution of reproducible and efficient depletion of blood plasma in a semi-automated manner.Entities:
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Year: 2006 PMID: 16414315 DOI: 10.1016/j.jchromb.2005.12.013
Source DB: PubMed Journal: J Chromatogr B Analyt Technol Biomed Life Sci ISSN: 1570-0232 Impact factor: 3.205