Efficient fabrication of high‐capacity immobilized metal ion affinity chromatographic media: The role of the dextran‐grafting process and its manipulation

Zhao, Lan; Zhang, Jingfei; Huang, Yongdong; Li, Qiang; Zhang, Rongyue; Zhu, K. J.; Suo, Jia; Su, Zhiguo; Zhang, Zhigang; Ma, Guanghui

doi:10.1002/jssc.201501291

Cited by 8 publications

(4 citation statements)

References 25 publications

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“…One gram of suction‐dried Sepharose 4FF ® was mixed with 0.2 mL of ECH in sodium hydroxide solution by agitation at 50°C overnight. Then, the activated microspheres were washed with distilled water and then 1 mL of aqueous Dextran T40 solution (0.6 g/mL) was added in sodium hydroxide solution . Dextran‐grafted microspheres were washed with distilled water and activated with ECH in sodium hydroxide solution at 30°C for 6 h .…”

Section: Methodsmentioning

confidence: 99%

“…Previous studies about dextran‐grafted chromatographic media focused on ion‐exchangers, studies were seldom reported dextran‐grafting process on affinity chromatographic media. In our group, novel dextran‐grafted metal chelating chromatographic medium was elaborately fabricated with binding capacity improved significantly . Whether the dextran‐grafting process is effective in enhancing the binding performance of affinity chromatographic media, and also, how the dextran‐grafting process improves the binding ability and the stability of the media are still unknown.…”

Section: Introductionmentioning

confidence: 99%

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Enhanced binding by dextran-grafting to Protein A affinity chromatographic media

et al. 2017

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The cover picture shows the binding of antibody molecules to dextran-grafted Protein A affinity chromatographic medium. On the left, a schematic diagram of dextran-grafted Protein A affinity chromatographic medium is depicted, showing antibody molecules (yellow) binding to Protein A ligands (green) coupled site-directed to dextran (dark blue)-grafted agarose-based matrix (light blue). On the top of the right, confocal laser scanning microscopy images illustrate that immunoglobulin G molecules entered in the medium completely. At the bottom of the right, an atom force microscopy image of dextran-grafted medium is presented, showing a very rough surface to support the binding results. Liquid Chromatography 1434 Effect of water on the retention on diol and amide columns in hydrophilic interaction liquid chromatography P. Jandera, P. Janás, V. Škeříková and J. Urban 1449 Phenolic composition of pomegranate peel extracts using an liquid chromatography-mass spectrometry approach with silica hydride columns 1457 Simultaneous quantitative determination of 11 sesquiterpene lactones in Jerusalem artichoke (Helianthus tuberosus L.) leaves by ultra high performance liquid chromatography with quadrupole time-of-flight mass spectrometry

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Enhanced binding by dextran-grafting to Protein A affinity chromatographic media

et al. 2017

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“…Confocal laser scanning microscopy evaluation CLSM has been popularly used for studying protein distribution when immobilized or bound to a chromatographic medium [31]. It provides the possibility of measuring the fluorescent emission of fluorescence dye within 3D objects with high local resolution and depth discrimination [32]. In this work, CLSM was used to visualize both nanodiscs coupling and CYP450 binding behavior in chromatographic medium (Figure 6).…”

Section: 6mentioning

confidence: 99%

Tailored nanodisc immobilization for one‐step purification and reconstitution of cytochrome P450: A tool for membrane proteins’ hard cases

Zhao

Tao

Huang

et al. 2021

J of Separation Science

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A novel nanodisc-based immobilization method was developed for high-efficient purification and reconstitution of cytochrome P450 in one step. Using membrane scaffold protein containing a histidine tag, charged-nanodiscs were prepared in the form of self-assembly of lipid-protein nanoparticles. Their properties including the particle diameter and its distribution and Zeta potential were controlled well by adjusting molar ratios of phospholipids to membrane scaffold protein. At an optimum lipid-to-membrane scaffold protein molar ratio of 60:1, uniformly regular-shaped and discoidal nanodiscs with an average particle diameter of 10 nm and Zeta potential of -19 mV were obtained. They can be well fractionated by size exclusion chromatography. Charged-nanodiscs were successfully immobilized onto Ni-chelating microspheres via histidine tags with a density of 6.6 mg membrane scaffold protein/mL gel. After being packed in a column, chromatography studies demonstrated that this nanodisc-immobilized chromatographic medium had a specific binding to cytochrome P450 in rat liver microsome. Nanodiscs containing cytochrome P450 can be furthermore eluted from the column with a diameter of about 87.0 nm and height of about 8.0 nm, respectively. The purity of cytochrome P450 after purification increased 25 folds strikingly. This nanodisc-immobilized chromatography method is promising for the one-step purification and reconstitution of membrane protein.

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“…Recently, polymer‐grafted chromatographic resins have been developed to improve the protein adsorption capacity and adsorption rates . These polymer‐grafted resins possess many polymer chains in the pores, which could provide 3‐D flexible binding for target protein and result in higher DBC than nongrafted resins . Dextran‐grafted resins are typical and could be prepared by the “grafting to” technique, i.e.…”

Section: Introductionmentioning

confidence: 99%

Poly(glycidyl methacrylate)‐grafted hydrophobic charge‐induction agarose resins with 5‐aminobenzimidazole as a functional ligand

Liu

Lin

Wang

et al. 2016

J of Separation Science

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Hydrophobic charge-induction chromatography is a new technology for antibody purification. To improve antibody adsorption capacity of hydrophobic charge-induction resins, new poly(glycidyl methacrylate)-grafted hydrophobic charge-induction resins with 5-aminobenzimidazole as a functional ligand were prepared. Adsorption isotherms, kinetics, and dynamic binding behaviors of the poly(glycidyl methacrylate)-grafted resins prepared were investigated using human immunoglobulin G as a model protein, and the effects of ligand density were discussed. At the moderate ligand density of 330 μmol/g, the saturated adsorption capacity and equilibrium constant reached the maximum of 140 mg/g and 25 mL/mg, respectively, which were both much higher than that of non-grafted resin with same ligand. In addition, effective pore diffusivity and dynamic binding capacity of human immunoglobulin G onto the poly(glycidyl methacrylate)-grafted resins also reached the maximum at the moderate ligand density of 330 μmol/g. Dynamic binding capacity at 10% breakthrough was as high as 76.3 mg/g when the linear velocity was 300 cm/h. The results indicated that the suitable polymer grafting combined with the control of ligand density would be a powerful tool to improve protein adsorption of resins, and new poly(glycidyl methacrylate)-grafted hydrophobic charge-induction resins have a promising potential for antibody purification applications.

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Efficient fabrication of high‐capacity immobilized metal ion affinity chromatographic media: The role of the dextran‐grafting process and its manipulation

Cited by 8 publications

References 25 publications

Enhanced binding by dextran-grafting to Protein A affinity chromatographic media

Enhanced binding by dextran-grafting to Protein A affinity chromatographic media

Tailored nanodisc immobilization for one‐step purification and reconstitution of cytochrome P450: A tool for membrane proteins’ hard cases

Poly(glycidyl methacrylate)‐grafted hydrophobic charge‐induction agarose resins with 5‐aminobenzimidazole as a functional ligand

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