1999
DOI: 10.1016/s0167-2991(99)80573-4
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Protein adsorption dissociation constants in various types of biochromatography

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Cited by 4 publications
(3 citation statements)
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“…In terms of the magnitude of the K values obtained in these experiments, there are, unfortunately, no directly comparable K values available in the literature. However, the order of magnitude of the K values obtained from these MALDI experiments is consistent with that of a large number of K values reported for other proteins on various surfaces . In addition, recent computational and experimental studies of the interaction of a small model peptide GGGKGGG, with the hydrophobic surface of a methyl-terminated self-assembled monolayer, yielded values of 1.1 × 10 4 and 1.1 × 10 5 L/mol, respectively. …”
Section: Resultssupporting
confidence: 87%
See 1 more Smart Citation
“…In terms of the magnitude of the K values obtained in these experiments, there are, unfortunately, no directly comparable K values available in the literature. However, the order of magnitude of the K values obtained from these MALDI experiments is consistent with that of a large number of K values reported for other proteins on various surfaces . In addition, recent computational and experimental studies of the interaction of a small model peptide GGGKGGG, with the hydrophobic surface of a methyl-terminated self-assembled monolayer, yielded values of 1.1 × 10 4 and 1.1 × 10 5 L/mol, respectively. …”
Section: Resultssupporting
confidence: 87%
“…The techniques used in the determination of equilibrium binding constants include chromatography, , radiotracer techniques, , electrophoresis, surface plasmon resonance spectroscopy, , colorimetric assays, , and fluorescence spectroscopy . Patel and Luo have summarized the equilibrium binding data obtained from biochromatography and developed a chart of relative protein adsorption strength …”
Section: Introductionmentioning
confidence: 99%
“…Crucial for specific affinity ligands is the consideration of their dissociation constants. For recombinant proteins, dissociation constants of 10 -4 -10 -10 M are usually considered a good working range [115]. Optimal affinity ligands allow fast binding kinetics for high flow rates but mild elution conditions to avoid reduction in immunogenicity or activity.…”
Section: Surface Chemistry Of the Stationary Phase And The Composition mentioning
confidence: 99%