Encyclopedia of Analytical Chemistry 2000
DOI: 10.1002/9780470027318.a0207
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High‐Performance Liquid Chromatography of Biological Macromolecules

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“…gel-permeation chromatography) and ion exchange chromatography (e.g. ion-exchange chromatography and ligand-exchange chromatography), because of its rapid, specific, sensitive and precise measurements [42].…”
Section: Gr Up Smmentioning
confidence: 99%
“…gel-permeation chromatography) and ion exchange chromatography (e.g. ion-exchange chromatography and ligand-exchange chromatography), because of its rapid, specific, sensitive and precise measurements [42].…”
Section: Gr Up Smmentioning
confidence: 99%
“…The most popular method for the chromatographic separation of peptides is reversed-phase high-performance liquid chromatography (RP-HPLC) applying hydrophobic stationary phases and gradients of acetonitrile in aqueous solutions as eluents. 12 Separations can be performed at both acidic 13 and alkaline pH, 14 and ion-pairing additives such as trifluoroacetic acid (TFA), 15,16 heptafluorobutyric acid (HFBA), 17 or triethylamine/acetic acid (TEA/HOAc) 18 have been utilized to enhance electrostatic interaction of the peptides with the stationary phase. Macroporous butyl or octadecyl silica stationary phases have been used for the separation of nonphosphorylated peptides from their phosphorylated analogues.…”
mentioning
confidence: 99%
“…Although the analysis of intact proteins embraces both primary amino acid sequence and posttranslational modifications, investigation at the level of peptide fragments is more established in terms of separation and characterization by MS and MS/MS, however, at the risk of not detecting the peptide containing the modification. The most popular method for the chromatographic separation of peptides is reversed-phase high-performance liquid chromatography (RP-HPLC) applying hydrophobic stationary phases and gradients of acetonitrile in aqueous solutions as eluents . Separations can be performed at both acidic and alkaline pH, and ion-pairing additives such as trifluoroacetic acid (TFA), , heptafluorobutyric acid (HFBA), or triethylamine/acetic acid (TEA/HOAc) have been utilized to enhance electrostatic interaction of the peptides with the stationary phase.…”
mentioning
confidence: 99%