1984
DOI: 10.1016/s0021-9673(01)96400-3
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Optimization model for the gradient elution separation of peptide mixtures by reversed-phase high-performance liquid chromatography

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Cited by 166 publications
(49 citation statements)
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“…At higher flow rates, and consequently higher shear forces, the protein tended to unfold, exposing more of its hydrophobic moiety that interacts with the reversed-phase stationary phase for increased retention. Similar results were found for carbonic anhydrase and other proteins [212].…”
Section: Effect Of Pressuresupporting
confidence: 87%
“…At higher flow rates, and consequently higher shear forces, the protein tended to unfold, exposing more of its hydrophobic moiety that interacts with the reversed-phase stationary phase for increased retention. Similar results were found for carbonic anhydrase and other proteins [212].…”
Section: Effect Of Pressuresupporting
confidence: 87%
“…To enhance interaction of hydrophilic peptides with the stationary phase the best thing to do when dealing with unknown peptide mixtures is to run water through the reversed-phase chromatographic column and inject the peptide mixture also dissolved in water or a buffer. If the peptide mixture contains a large number of peptides, the aqueous solvent has to be replaced by the organic solvent very slowly to guarantee peak separation and proper identification (Stadalius et al 1985).…”
Section: Reversed-phase Chromatographymentioning
confidence: 99%
“…For e > e~.r, retention of macromolecules is dominated by adsorption ( Figure 2). 6. Starting from a certain e value, apparent recovery of high molar mass samples decreases (Figures 1, 3 and 4) and, eventually, polymer species are fully retained within given column and eluent and at a given temperature.…”
mentioning
confidence: 92%
“…For example, Snyder et al [6,7] applied theoretical backgrounds of HPLC of small molecules and Armstrong and Boehm included also some pecularities of polymer solutions [8].…”
Section: Introductionmentioning
confidence: 99%