“…Many proteins were purified from blood fluids using sequential chromatography (Duckert, Koller, & Matter, 1953;Kanai, Raz, & Goodman, 1968;McConnell & Mason, 1970;Murthy & Hercz, 1973;Poffenbarger, 1975;Tollefsen, Majerus, & Blank, 1982). Proteins have been examined by partition chromatography prior to MS/MS using resins such as: Heparin (Tollefsen, Majerus, & Blank, 1982;Capila & Linhardt, 2002;Saito & Munakata, 2007;Lei et al, 2008); weak anion exchangers such as DEAE (Marshall et al, 2003; strong anion exchangers such as Quaternary Amine (Vasileva, Jakab, & Hasko, 1981;Sahab, Iczkowski, & Sang, 2007;Kovac et al, 2008); strong cation exchangers like propyl sulfate (Pieper et al, 2003a), carbohydrate binding columns like concanavalin A (Kass, Ratnoff, & Leon, 1969;Murthy & Hercz, 1973); size fractionation, hydrophobic interaction (Ruhaak et al, 2008), size exclusion, hydrophilic zwitterionic resins (Intoh et al, 2009), protein G resin (Neubert & James, 2009), size exclusion or gel filtration (Ratnoff, Kass, & Lang, 1969;Gao et al, 2005a;Hortin et al, 2006;Tucholska et al, 2007) or a battery of disposable preparative resins Tucholska et al, 2009). The use of LC to ESI-TOF to obtain intact protein molecular masses in combination with digestion and LC-ESI-MS/MS of the same fractions has been suggested as a way to obtain protein and peptide information from blood samples (Chen et al, 2007a).…”