Adsorption and elution of bovine γ-globulin using an affinity membrane containing hydrophobic amino acids as ligands

Kim, Min; Saito, Kyoichi; Furusaki, Shintaro; Sato, Takeshi; Sugo, Takanobu; Ishigaki, Isao

doi:10.1016/0021-9673(91)85055-k

Cited by 111 publications

(39 citation statements)

References 10 publications

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“…An affinity system using stacked membranes in this study has a considerably sharper breakthrough curve than one using hollow fibers, as shown by data from Kim et al (1991) andfrom lwata et al (1991). This behavior can be explained on the basis of the following analysis.…”

Section: Calculation Of Breakthrough Curves With Stacked Membranessupporting

confidence: 58%

Breakthrough of lysozyme through an affinity membrane of cellulose‐cibacron blue

Liu

Fried

1994

AIChE Journal

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The dynamic affinity adsorption of lysozyme through stacked flat-sheet cellulose membranes with immobilized cibacron blue 3GA was studied and compared to three affinity-membrane models: diffusion model to explore the importance of axial and radial diffusion; variation model to study the effects of pore-size distribution or thickness variation; and stack model to investigate the effects of stacking flat-sheet membranes. For the diffusion model, when Per> 0.1, radial diffusional resistance is significant, but when Pe, < 25, axial dispersion must be considered. For the variation model, increasing pore-size distribution or nonuniform membrane thickness greatly broadens the breakthrough curve. The stack model shows that the stacking of membranes significantly sharpens the breakthrough curves by averaging out the flow dispersion due to pore-size distribution or thickness variation.

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Section: Calculation Of Breakthrough Curves With Stacked Membranessupporting

confidence: 58%

Breakthrough of lysozyme through an affinity membrane of cellulose‐cibacron blue

Liu

Fried

1994

AIChE Journal

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“…Kim et al used hydrophobic amino acids (e.g., phenylalanine and tryptophan) containing membranes based on polyethylene and they obtained 50 mg N (g polymer) -1 for bovine gamma globulin. [22] Müller-Schulte et al used several polymeric carriers made of different polymers including Biograft, Sepharose 4B, Superose and Spherosil and histidine as the pseudospecific ligand. [23] Their maximum IgG 1 adsorption values were in the range of 0.05-0.23 (mg IgG 1 ) N (mL sorbent) -1 .…”

Section: Comparison With Related Literaturementioning

confidence: 99%

A Novel Affinity Support Material for the Separation of Immunoglobulin G from Human Plasma

Gari̇pcan

Deni̇zli̇²

2002

Macromol. Biosci.

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2‐Methacrylamidohistidine (MAH) as a pseudospecific ligand was synthesized from methacryl chloride and histidine. Spherical beads with an average size of 50–63 μm were obtained by the radical suspension polymerization of MAH and 2‐hydroxyethyl methacrylate (HEMA) conducted in an aqueous dispersion medium. Owing to the reasonably rough character of the bead surface, P(HEMA‐co‐MAH) beads had a specific surface area of 17.6 m2·g–1. Synthesized MAH was characterized by NMR. P(HEMA‐co‐MAH) beads were characterized by swelling studies, FT‐IR spectroscopy, scanning electron microscopy (SEM) and elemental analysis. P(HEMA‐co‐MAH) affinity beads with a swelling ratio of 65% were used in the separation of human immunoglobulin G (HIgG) from aqueous solutions and human plasma. The maximum HIgG adsorption on the P(HEMA‐co‐MAH) adsorbents was observed at pH 7.4 for phosphate and at pH 6.0 for morpholinoethanesulfonic acid buffers. The HIgG adsorption onto the PHEMA adsorbents was negligible. Higher adsorption values (up to 46.5 mg·g–1) were obtained when the P(HEMA‐co‐MAH) adsorbents were used in aqueous solutions. Much higher amounts of HIgG were adsorbed from human plasma (up to 73.8 mg·g–1). Adsorption capacities of other blood proteins were obtained as 3.2 mg·g–1 for fibrinogen and 4.6 mg·g–1 for albumin. The total protein adsorption was determined to be 82.2 mg·g–1. The pseudospecific affinity beads allowed one‐step separation of HIgG from human plasma. HIgG molecules could be repeatedly adsorbed and desorbed with these adsorbents without noticeable loss in their HIgG adsorption capacity.

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“…2 for details). In further experiments we found that XL Y does not bind nonspecifically to unrelated proteins such as bovine gamma globulin that display affinity for hydrophobic surfaces (62) (Fig. 3G).…”

Section: Resultsmentioning

confidence: 99%

Unraveling the Mechanism of a Potent Transcriptional Activator

Lü¹,

Rowe

Brennan

et al. 2005

Journal of Biological Chemistry

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Despite their enormous potential as novel research tools and therapeutic agents, artificial transcription factors (ATFs) that up-regulate transcription robustly in vivo remain elusive. In investigating an ATF that does function exceptionally well in vivo, we uncovered an unexpected relationship between transcription function and a binding interaction between the activation domain and an adjacent region of the DNA binding domain. Disruption of this interaction leads to complete loss of function in vivo, even though the activation domain is still able to bind to its target in the transcriptional machinery. We propose that this interaction parallels those between natural activation domains and their regulatory proteins, concealing the activation domain from solvent and the cellular milieu until it binds to its transcriptional machinery target. Inclusion of this property in the future design of ATFs should enhance their efficacy in vivo.

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Adsorption and elution of bovine γ-globulin using an affinity membrane containing hydrophobic amino acids as ligands

Cited by 111 publications

References 10 publications

Breakthrough of lysozyme through an affinity membrane of cellulose‐cibacron blue

Breakthrough of lysozyme through an affinity membrane of cellulose‐cibacron blue

A Novel Affinity Support Material for the Separation of Immunoglobulin G from Human Plasma

Unraveling the Mechanism of a Potent Transcriptional Activator

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