On-line microdialysis of proteins with high-salt buffers for direct coupling of electrospray ionization mass spectrometry and liquid chromatography

Methods for samples preparation in proteomic research

“…is less frequently used [384], since they require non-volatile inorganic buffers. Nevertheless, these types of chromatography are often used in biochemical purifications (using volatile buffers that overcome such problems) as they preserve the function of proteins, therefore, in order to facilitate ESI-MS analysis of eluents, on-line desalting methods were developed based on microdialysis [385], or other principles [186,386].…”

The effect of the mobile phase additives on sensitivity in the analysis of peptides and proteins by high-performance liquid chromatography–electrospray mass spectrometry

“…Canarelli et al [95] also developed a microdialysis system allowing the on-line coupling of ESI-MS with LC methods requiring the use of salts. They applied this system to the separation of proteins by affinity chromatography-, IEC-, and SEC-ESI-MS.…”

Subproteomics in Analytical Chemistry: Chromatographic Fractionation Techniques in the Characterization of Proteins and Peptides

“…Size exclusion chromatography has been used to fractionate human serum in the analysis of the glycoprotein prostate specific antigen (PSA). [26] Size exclusion chromatography is an effective way to obtain low molecular weight fractions of proteins and peptides, namely those under 20 kD that do not run well on 2D gels due to the low molecular weight. The outer surface of the RAM material is coated with hydrophilic hydroxyl groups while the internal surface of the pores are coated with a chromatographic functionality, such as an ion exchanger or reverse-phase chemistry such as C 18 .…”