Interactions of Imidazole and Proteins with Immobilized Cu(II) Ions: Effects of Structure, Salt Concentration, and pH in Affinity and Binding Capacity

Chen, Wen Yih; Wu, Ching Fa; Liu, Chih Chung

doi:10.1006/jcis.1996.0283

Cited by 65 publications

(39 citation statements)

References 9 publications

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“…Depending on the location of the surfaceaccessible groups of the protein, a maximum in the association constant will occur when the distribution of the ligands on the chromatographic surface optimally mirrors in a complementary context this three-dimensional arrangement. Similar conclusions have recently been reached by other investigators for the interaction of proteins with IMAC adsorbents (34)(35)(36). Changes in ionic strength, pH, or temperature which affect the three-dimensional arrangement of these interacting groups will thus influence the shape of the adsorption isotherm.…”

Section: Resultssupporting

confidence: 60%

Protein Interaction with Immobilized Metal Ion Affinity Ligands under High Ionic Strength Conditions

Jiang

Hearn

1996

Analytical Biochemistry

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Section: Resultssupporting

confidence: 60%

Protein Interaction with Immobilized Metal Ion Affinity Ligands under High Ionic Strength Conditions

Jiang

Hearn

1996

Analytical Biochemistry

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“…Chen et al investigated lysozyme adsorption capacity on the hydrophilic gel; the maximum lysozyme adsorption capacity of the adsorbents was 84 mg/g. 19 Horstman et al reported 15.1-16.6 mg/g lysozyme adsorption on the Cibacron Blue F3GA-Sepharose CL-6B. 20 Nash and Chase modified the poly(styrenedivinylbenzene) chromatography matrices by the adsorption and crosslinking of poly(vinyl alcohol), and they attached Procion Yellow HE-3G dyeligand for human serum albumin and lysozyme adsorption.…”

Section: Effect Of Cu(ii)-incorporationmentioning

confidence: 98%

“…While maintaining a free cysteine residue in a natural protein is rare, 18 the exposed histidine residue is the dominant binding site in protein adsorption with an immobilized metal ion. 19 Chicken egg white lysozyme consists of 129 amino acids and contains four disulfide bridges. Factors influencing the interactions include the number of electron-donating groups on the protein surface, medium pH, concentration of protein, type of metal ions, ligand density, and type and size of chelating ligand.…”

Section: Effect Of Cu(ii)-incorporationmentioning

confidence: 99%

Nonporous monosize polymeric sorbents: Dye and metal chelate affinity separation of lysozyme

Deni̇zli̇

Yavuz

Gari̇pcan

et al. 2000

J. Appl. Polym. Sci.

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Lysozyme adsorption onto dye-attached nonporous monosize poly(2-hydroxyethyl-methacrylate-methylmethacrylate) [poly(HEMA-MMA)] microspheres was investigated. Poly(HEMA-MMA) microspheres were prepared by dispersion polymerization. The monochloro-triazine dye, Cibacron Blue F3GA, was immobilized covalently as dye-ligand. These dye-affinity microspheres were used in the lysozyme adsorptiondesorption studies. The effect of initial concentration of lysozyme and medium pH on the adsorption efficiency of dye-attached and metal-chelated microspheres were studied in a batch reactor. Effect of Cu(II) chelation on lysozyme adsorption was also studied. The nonspecific adsorption of lysozyme on the poly(HEMA-MMA) microspheres was 3.6 mg/g. Cibacron Blue F3GA attachment significantly increased the lysozyme adsorption up to 247.8 mg/g. Lysozyme adsorption capacity of the Cu(II) incorporated microspheres (318.9 mg/g) was greater than that of the Cibacron Blue F3GA-attached microspheres. Significant amount of the adsorbed lysozyme (up to 97%) was desorbed in 1 h in the desorption medium containing 1.0M NaSCN at pH 8.0 and 25 mM EDTA at pH 4.9. In order to examine the effects of separation conditions on possible conformational changes of lysozyme structure, fluorescence spectrophotometry was employed. We conclude that dye-and metal-chelate affinity chromatography with poly(HEMA-MMA) microspheres can be applied for lysozyme separation without causing any significant changes and denaturation. Repeated adsorption/desorption processes showed that these novel dye-attached monosize microspheres are suitable for lysozyme adsorption.

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“…butions toward the interaction of immobilized metal ion with imidazole and proteins (16,17). However, the imidazole The ligand affinity technique displays a high selectivity group of the histidine residue is the major functional group for biological separation.…”

Section: Introductionmentioning

confidence: 99%

“…The direct enthalpy measurement of the interaction pro-of protein by immobilized ions remains unclear. In the pro- tein surface, the pH value of the interaction, the salt type Key Words: immobilized metal ion affinity; microcalorimetry; and concentration (16,17), the temperature (15, 16), the adsorption; imidazole; IMA.protein structure, the surface chemistry, and the degree of hydration of the protein.Previous literatures have established those factors' contri- …”

mentioning

confidence: 99%

Microcalorimetric Studies of the Interactions of Imidazole with Immobilized Cu(II): Effects of pH Value and Salt Concentration

Chen

Lee

1996

Journal of Colloid and Interface Science

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ions frequently varies with the topography of the protein In this investigation, we measured the influence of pH value surface and the chemistry and physical conditions of the and salt concentration on the heat of interaction between imidazole interaction conditions. Although mechanisms have been proand CS-IDA-Cu(II) gel with a highly sensitive microcalori-posed for IMA with protein, the macromolecular recognition meter. The direct enthalpy measurement of the interaction pro-of protein by immobilized ions remains unclear. In the pro- tein surface, the pH value of the interaction, the salt type Key Words: immobilized metal ion affinity; microcalorimetry; and concentration (16,17), the temperature (15, 16), the adsorption; imidazole; IMA.protein structure, the surface chemistry, and the degree of hydration of the protein.Previous literatures have established those factors' contri-

show abstract

Interactions of Imidazole and Proteins with Immobilized Cu(II) Ions: Effects of Structure, Salt Concentration, and pH in Affinity and Binding Capacity

Cited by 65 publications

References 9 publications

Protein Interaction with Immobilized Metal Ion Affinity Ligands under High Ionic Strength Conditions

Protein Interaction with Immobilized Metal Ion Affinity Ligands under High Ionic Strength Conditions

Nonporous monosize polymeric sorbents: Dye and metal chelate affinity separation of lysozyme

Microcalorimetric Studies of the Interactions of Imidazole with Immobilized Cu(II): Effects of pH Value and Salt Concentration

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