Modification of polystyrenic matrices for the purification of proteins

Nash, Dominic C; Chase, Howard A.

doi:10.1016/s0021-9673(97)00469-x

Cited by 32 publications

(8 citation statements)

References 17 publications

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“…A significant change in original surface characteristics through dye coupling has been achieved. Rubisco adsorbs more on the dyed surface, suggesting higher protein affinity for the dye, which is in agreement with observations by other researchers for other proteins [18,30,[39][40][41][42][43][44][45][46]. Fig.…”

Section: Resultssupporting

confidence: 91%

The construction, fouling and enzymatic cleaning of a textile dye surface

Onaizi

Middelberg

2010

Journal of Colloid and Interface Science

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Section: Resultssupporting

confidence: 91%

The construction, fouling and enzymatic cleaning of a textile dye surface

Onaizi

Middelberg

2010

Journal of Colloid and Interface Science

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“…25 Nash and Chase modified poly(styrene-divinyl benzene) microspheres using PVA and Procion Blue MX-R, Procion Red HE-3B, Procion Yellow HE-3G, and Cibacron Blue F3GA dye ligands. 26 They presented adsorption capacities of 11.7-27 mg HSA/g. Horstmann et al presented adsorption capacities of 5.4 -11.2 mg BSA/g with the Cibacron Blue F3GA attached Sepharose CL-6B.…”

Section: Effect Of Bsa Initial Concentrationmentioning

confidence: 99%

Dye-ligand column chromatography: Albumin adsorption from aqueous media and human plasma with dye-affinity microbeads

Deni̇zli̇

Köktürk

Yavuz

et al. 1999

J. Appl. Polym. Sci.

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Cibacron Blue F3GA was covalently coupled with poly(ethylene glycoldimethacrylate-2-hydroxyethylmethacrylate) [poly(EGDMA-HEMA)] microbeads via the nucleophilic substitution reaction between the chloride of its triazine ring and the hydroxyl groups of the HEMA molecules under alkaline conditions. The affinity sorbent carrying 16.5 mol Cibacron Blue F3GA/g polymer was then used for bovine serum albumin (BSA) adsorption from aqueous protein solutions and from human plasma in a packed-bed column. The BSA adsorption capacity of the microbeads decreased with an increase in the recirculation rate. High adsorption rates were observed at the beginning, then equilibrium was gradually achieved in about 60 min. The BSA concentration in the mobile phase was also effective on adsorption. BSA adsorption was first increased with BSA concentration, then reached a plateau that was about 57.3 mg BSA/g. Higher BSA adsorption was observed at lower ionic strength. The maximum adsorption was observed at pH 5.0, which is the isoelectric pH of BSA. Higher human serum albumin adsorption was achieved from human plasma (109.6 mg HSA/g). High desorption ratios (over 94% of the adsorbed albumin) were achieved by using 1.0M NaSCN (pH 8.0) in 30 min. It was observed that albumin could be repeatedly adsorbed and desorbed without a significant loss in adsorption capacity.

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“…Denizli et al used dye and metal‐chelate sorbents including monosize poly(methyl methacrylate–hydroxyethyl methacrylate), PVAL, and poly(hydroxyethyl methacrylate) beads and they obtained 35–178 mg per gram polymer for HSA 24–28. Nash and Chase used PVAL‐modified poly(styrene–divinylbenzene) beads carrying different dye ligands 29. They presented adsorption capacities of 11.7–27 mg HSA/g.…”

Section: Resultsmentioning

confidence: 99%

Preparation of a novel metal‐chelate affinity beads for albumin isolation from human plasma

Odabaşı

Gari̇pcan

Deni̇zli̇

2003

J of Applied Polymer Sci

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ABSTRACT:In this study, we developed a novel approach to obtain a high protein-adsorption capacity utilizing 2-methacryloylamidohistidine (MAH) as a biollgand. MAH was synthesized by reacting methacryloyl chloride and histidine. Spherical beads, with an average size of 150 -200 m, were obtained by the radical suspension polymerization of MAH, ethyleneglycol dimethacrylate (EGDMA), and 2-hydroxyethyl methacrylate (HEMA) conducted in an aqueous dispersion medium. p(EGDMA-HEMA-MAH) beads had a specific surface area of 17.6 m 2 /g. The synthesized MAH monomer was characterized by NMR. p(EGDMA-HEMA-MAH) beads were characterized by a swelling test, FTIR, and elemental analysis. Then, Cu(II) ions were incorporated into the beads and Cu(II) loading was found to be 0.96 mmol/g. These beads, with a swelling ratio of 65% and containing 1.6 mmol MAH/g, were used in the adsorption/ desorption of human serum albumin (HSA) from both aqueous solutions and human serum. The adsorption of HSA onto p(EGDMA-HEMA-MAH) was low (8.8 mg/g). Cu(II) chelation onto the beads significantly increased the HSA adsorption (56.3 mg/g). The maximum HSA adsorption was observed at pH 8.0 Higher HSA adsorption was observed from human serum (94.6 mg HSA/g). Adsorptions of other serum proteins were obtained as 3.7 mg/g for fibrinogen and 8.5 mg/g for ␥-globulin. The total protein adsorption was determined as 107.1 mg/g. Desorption of HSA was obtained using a 0.1M Tris/HCI buffer containing 0.5M NaSCN. High desorption ratios (to 98% of the adsorbed HSA) were observed. It was possible to reuse Cu(II)-chelated p(EGDMA-HEMA-MAH) beads without significant decreases in the adsorption capacities.

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Modification of polystyrenic matrices for the purification of proteins

Cited by 32 publications

References 17 publications

The construction, fouling and enzymatic cleaning of a textile dye surface

The construction, fouling and enzymatic cleaning of a textile dye surface

Dye-ligand column chromatography: Albumin adsorption from aqueous media and human plasma with dye-affinity microbeads

Preparation of a novel metal‐chelate affinity beads for albumin isolation from human plasma

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