Improving Proteome Coverage by Reducing Sample Complexity via Chromatography
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Springer International Publishing
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http://link.springer.com/content/pdf/10.1007/978-3-319-41448-5_5
Reference188 articles.
1. Aguilar M-I (2004) HPLC of peptides and proteins. HPLC of peptides and proteins, vol 251 M-I Aguilar. Springer, New York, p 3–8
2. Aguilar MI, Hearn MT (1996) High-resolution reversed-phase high-performance liquid chromatography of peptides and proteins. Methods Enzymol 270:3–26
3. Allen DP (1999) 18 – Application of size exclusion-high-performance liquid chromatography for biopharmaceutical protein and peptide therapeutics. Column handbook for size exclusion chromatography. Cs Wu. Academic Press, San Diego, 531–537
4. Alpert AJ (1983) Cation-exchange high-performance liquid chromatography of proteins on poly(aspartic acid)—silica. J Chromatogr A 266(0):23–37 A simple cation-exchange material for high-performance liquid chromatography of proteins was developed. Poly(succinimide) reacted rapidly with aminopropylsilica and the product was hydrolysed to poly(aspartic acid)—silica. Reaction conditions were optimized to yield a material with an ion-exchange capacity of 430 mg hemoglobin/g material. High-performance liquid chromatographic columns of the material featured excellent performance in terms of capacity, selectivity, recovery of enzyme activity, peak shape and durability. Protein standards and clinical hemoglobin samples were well resolved in minutes. Poly(succinimide)—silica was readily derivatized to give products other than poly(aspartic acid)—silica, and several such materials were prepared. Such materials could be useful for affinity chromatography or enzyme immobilization.
5. Alpert AJ (1990) Hydrophilic-interaction chromatography for the separation of peptides, nucleic acids and other polar compounds. J Chromatogr A 499(0):177–196 When a hydrophilic chromatography column is eluted with a hydrophobic (mostly organic) mobile phase, retention increases with hydrophilicity of solutes. The term hydrophilic-interaction chromatography is proposed for this variant of normal-phase chromatography. This mode of chromatography is of general utility. Mixtures of proteins, peptides, amino acids, oligonucleotides, and carbohydrates are all resolved, with selectivity complementary to those of other modes. Typically, the order of elution is the opposite of that obtained with reversed-phase chromatography. A hydrophilic, neutral packing was developed for use in high-performance hydrophilic-interaction chromatography. Hydrophilic-interaction chromatography is particularly promising for such troublesome solutes as histones, membrane proteins, and phosphorylated amino acids and peptides. Hydrophilic-interaction chromatography fractionations resemble those obtained through partitioning mechanisms. The chromatography of DNA, in particular, resembles the partitioning observed with aqueous two-phase systems based on polyethylene glycol and dextran solutions.
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