2009
DOI: 10.1002/bmc.1159
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Separation with zwitterionic hydrophilic interaction liquid chromatography improves protein identification by matrix‐assisted laser desorption/ionization‐based proteomic analysis

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Cited by 24 publications
(20 citation statements)
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“…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).…”
Section: Partition Chromatography Of Proteins and Peptidesmentioning
confidence: 99%
“…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).…”
Section: Partition Chromatography Of Proteins and Peptidesmentioning
confidence: 99%
“…The most common stationary phases applied for peptide separation in HILIC mode include underivatized silica that contain functional groups such as siloxane, silanols and a small quantity of metals [141,142], and derivatized silica, which can be neutral stationary phases, such as TSKgel Amide-80; [138] ionic stationary phases, such as the weak cation-exchanger PolyCAT A [143], the cation exchanger polysulphoethyl A [133], the weak anion exchanger PolyWAX LP; [127] zwitterionic stationary phases, such as ZIC-HILIC [144,145] and ZIC-cHILIC [54]. Each of these materials is capable of generating a semi-immobilized aqueous layer on their polar surface [133].…”
Section: Hydrophilic Interactions Chromatography (Hilic)mentioning
confidence: 99%
“…Therefore, a digested peptide mixture should be well fractionated and concentrated for efficient protein identification with low background noise. We have previously reported an improved method for MALDI-TOF based proteomic analysis of membrane proteins with a combination of zwitterionic hydrophilic interaction liquid chromatography and reverse-phase chromatography, which is a more effective separation method for digested peptide mixtures (Intoh, et al, 2009a). Using this method, we have performed proteomic analysis of membrane proteins specifically expressed in pluripotent mouse ES cells.…”
Section: Proteomics Approaches To Identify Cell-surface Markers In Plmentioning
confidence: 99%