Separation of immunoglobulin G from human serum by pseudobioaffinity chromatography using immobilized l-histidine in hollow fibre membranes

Bueno, Sônia Maria Alves; Haupt, Karsten; Vijayalakshmi, M.A.

doi:10.1016/0378-4347(94)00601-z

Cited by 103 publications

(56 citation statements)

References 11 publications

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“…The K d values indicated that a moderate affinity is consistent with the easy and nondenaturing desorption of the bound HIgG and advantageous for the good recovery of nondenatured proteins. 30 The correlation coefficients of semireciprocal plots (R 2 ) was greater than 0.995 for poly(GMA/MMA/EGDMA)-AA and poly (GMA/ MMA/EGDMA)-SA affinity beads (Tables II and III), respectively.…”

Section: Adsorption Kinetic and Isotherm Modelsmentioning

confidence: 91%

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Adsorption of IgG on spacer‐arm and L‐arginine ligand attached poly(GMA/MMA/EGDMA) beads

Bayramoğlu

Şenel

Arıca

2007

J of Applied Polymer Sci

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This work presents data on human immunoglobulin G (HIgG) adsorption onto L‐arginine ligand attached poly(GMA/MMA/EGDMA)‐based affinity beads which were synthesized from methyl methacrylate (MMA) and glycidiyl methacrylate (GMA) in the presence of a crosslinker (i.e., ethylene glycol dimethacrylate; EGDMA) by suspension polymerization. The epoxy groups of the poly(GMA/MMA/EGDMA) beads were converted into amino groups after reaction with ammonia or 1,6‐diaminohexane (i.e., spacer‐arm). With L‐arginine as a ligand, it was covalently immobilized on the aminated (poly(GMA/MMA/EGDMA)‐ AA) and/or the spacer‐arm attached (poly(GMA/MMA/EGDMA)‐SA) beads, using glutaric dialdehyde as a coupling agent. Both affinity poly(GMA/MMA/EGDMA)‐based beads were used in HIgG adsorption/desorption studies under defined pH, ionic strength, or temperature conditions in a batch reactor, using acid‐treated poly(GMA/MMA/EGDMA) beads as a control system. The poly(GMA/MMA/EGDMA)‐SA affinity beads resulted in an increase in the adsorption capacity to HIgG compared with the aminated counterpart (i.e., poly(GMA/MMA/EGDMA)‐AA). The maximum adsorption capacities of the poly(GMA/MMA/EGDMA)‐AA and poly(GMA/MMA/EGDMA)‐SA affinity beads were found to be 112.36 and 142 mg g−1, and the affinity constants (Kd), evaluated by the Langmuir model, were 2.48 × 10−7 and 6.98 × 10−7M, respectively. Adsorption capacities of the poly(GMA/MMA/EGDMA)‐AA and poly(GMA/MMA/EGDMA)‐SA were decreased with HIgG by increasing the ionic strength adjusted with NaCl. Adsorption kinetic of HIgG onto both affinity adsorbents was analyzed with first‐ and second‐order kinetic equations. The first‐order equation fitted well with the experimental data. © 2007 Wiley Periodicals, Inc. J Appl Polym Sci 104: 672–679, 2007

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Section: Adsorption Kinetic and Isotherm Modelsmentioning

confidence: 91%

“…29,30 The optimal pH values for adsorption of HIgG on the affinity beads were investigated in the pH range of 4.0-8.0 (Fig. 2).…”

Section: Spacer-arm and Poly(gma/mma/egdma) Beadsmentioning

confidence: 99%

Adsorption of IgG on spacer‐arm and L‐arginine ligand attached poly(GMA/MMA/EGDMA) beads

Bayramoğlu

Şenel

Arıca

2007

J of Applied Polymer Sci

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“…9. The separation process was completed within 10 min, which was much faster than that was reported by Bueno et al (1995). Comparing the chromatograms shown in Figs.…”

Section: Resultsmentioning

confidence: 94%

High‐performance affinity chromatography with immobilization of protein A and L‐histidine on molded monolith

Luo

Zou

Zhang

et al. 2002

Biotech & Bioengineering

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Reactive monoliths of macroporous poly(glycidyl methacrylate-co-ethylene dimethacrylate) have been prepared by "in-situ" copolymerization of the monomers in the presence of porogenic diluents. Protein A and L-histidine were immobilized on the monoliths directly or through a spacer arm, respectively. The properties of these two kinds of affinity columns were characterized, and the results showed that the columns with coupling of ligands by a spacer arm have some extent of non-specific adsorption for bovine serum albumin. The affinity column based on the monolithic polymer support provided us with good hydrodynamic characteristic, low flow resistance, and easy preparation. These two affinity columns were used for the purification of immunoglobulin G from human serum. The purity of the purified IgG was detected by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS). The stability of the protein A affinity column was investigated, and its performance remained invariable after half a year. The effects of the nature and the pH of the buffer system on the adsorption capacity of human IgG on histidyl affinity column were also investigated. The protein A affinity column is favorable for rapid analysis of human IgG samples. In contrast, the advantages of mild elution conditions, high stability, as well as low cost provide the histidyl column further potential possibility for fast removal of IgG from human plasma in clinical applications.

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“…Bisoxirane was selected since it is a larger molecule compared to epibromohydrin and hence a more suitable spacer, providing better contact between the ligand (histidine) and the product (endotoxin) (Bueno, Haupt, Vijayalakshmi, 1995). The fourth step involves the reaction between histidine and bisoxirane (Figures 2(b) and 2(c)).…”

Section: Membrane Adsorbermentioning

confidence: 99%

Membrane adsorber for endotoxin removal

Almeida

Fingola

et al. 2016

Braz. J. Pharm. Sci.

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The surface of flat-sheet nylon membranes was modified using bisoxirane as the spacer and polyvinyl alcohol as the coating polymer. The amino acid histidine was explored as a ligand for endotoxins, aiming at its application for endotoxin removal from aqueous solutions. Characterization of the membrane adsorber, analysis of the depyrogenation procedures and the evaluation of endotoxin removal efficiency in static mode are discussed. Ligand density of the membranes was around 7 mg/g dry membrane, allowing removal of up to 65% of the endotoxins. The performance of the membrane adsorber prepared using nylon coated with polyvinyl alcohol and containing histidine as the ligand proved superior to other membrane adsorbers reported in the literature. The lack of endotoxin adsorption on nylon membranes without histidine confirmed that endotoxin removal was due to the presence of the ligand at the membrane surface. Modified membranes were highly stable, exhibiting a lifespan of approximately thirty months.Uniterms: Endotoxins/removal. Membrane adsorber/performance. Histidine. Poly(vinyl alcohol).A superfície de membranas planas de nylon foi modificada utilizando-se bisoxirano como espaçador e poli(álcool vinílico) para recobrimento das membranas. O aminoácido histidina foi utilizado como ligante para endotoxinas, visando à sua aplicação na remoção de endotoxinas a partir de soluções aquosas. São discutidas as etapas de caracterização do adsorvedor com membranas, análise do procedimento de despirogenização e avaliação da eficiência de remoção em modo estático. A densidade de ligantes nas membranas foi em torno de 7 mg/g membrana (massa seca), permitindo uma remoção de endotoxinas de até 65%. O desempenho das membranas preparadas com nylon e recobertas com poli(álcool vinílico) contendo histidina como ligante foi superior ao de outros adsorvedores com membranas descritos na literatura. A ausência de adsorção de endotoxinas em membranas sem histidina confirma que a remoção das endotoxinas deve-se exclusivamente à presença do ligante na superfície da membrana. As membranas modificadas mostraram-se bastante estáveis, exibindo um tempo de vida superior a 30 dias.Unitermos: Endotoxinas/remoção. Membrana adsorvente/desempenho. Histidina. Poli(álcool vinílico).

show abstract

Separation of immunoglobulin G from human serum by pseudobioaffinity chromatography using immobilized l-histidine in hollow fibre membranes

Cited by 103 publications

References 11 publications

Adsorption of IgG on spacer‐arm and L‐arginine ligand attached poly(GMA/MMA/EGDMA) beads

Adsorption of IgG on spacer‐arm and L‐arginine ligand attached poly(GMA/MMA/EGDMA) beads

High‐performance affinity chromatography with immobilization of protein A and L‐histidine on molded monolith

Membrane adsorber for endotoxin removal

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