Bilirubin and tryptophan adsorption in albumin-containing solutions

Annesini, Maria Cristina; Carlo, Chiara Di; Piemonte, Vincenzo; Turchetti, Luca

doi:10.1016/j.bej.2007.12.010

Cited by 36 publications

(33 citation statements)

References 23 publications

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“…Albumin, which is composed of 584 amino acid residues with a molecular weight of approximately 66,000 Da, was the natural carrier of bilirubin in blood. Each BSA molecule might have 12 binding sites to bilirubin, but only two of them bound bilirubin molecules tightly [33]. Adsorption experiments of P-A-HDA, P-B-HDA and P-A-G were performed by adding particles to previously prepared bilirubin solutions, with an initial concentration of 150 mg/L of BSA.…”

Section: Effect Of Bsa In the Adsorption Medium On Bilirubin Adsorptionmentioning

confidence: 99%

Functional polyethersulfone particles for the removal of bilirubin

Jiang

Xiang

Xie

et al. 2015

J Mater Sci: Mater Med

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In this study, polyethersulfone/poly (glycidyl methacrylate) particles are prepared via in situ cross-linked polymerization coupled with a phase inversion technique. The surfaces of these particles are then further modified by grafting amino groups using tetraethylenepentamine, dethylenetriamine, ethylenediamine, or 1,6-hexanediamine for the removal of bilirubin. The particles are characterized by Flourier transform infrared spectroscopy, thermogravimetric analysis, and scanning electron microscopy. Batch adsorption experiments are performed to verify the adsorption capability, and the effect of bilirubin initial concentration, bovine serum albumin concentration, and solution ionic strength on the adsorption is also investigated. In addition, both adsorption kinetic and isotherm models are applied to analyze the adsorption process of bilirubin, and a particle column is used to further study the bilirubin removal ability.To prove that the method was a universal portal to prepare functional particles, polysulfone, polystyrene, and poly(vinylidene fluoride) based functional particles were also prepared and used for the removal of bilirubin. This study and the results indicated that the particles had a great potential to be used in hemoperfusion treatment for hyperbilirubinemia.

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Section: Effect Of Bsa In the Adsorption Medium On Bilirubin Adsorptionmentioning

confidence: 99%

Functional polyethersulfone particles for the removal of bilirubin

Jiang

Xiang

Xie

et al. 2015

J Mater Sci: Mater Med

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“…Preliminary tests showed the adsorption process was completed in 2 hours. The amount of adsorption at equilibrium, q e was obtained by: (8) where C 0 and C e (mg/L) are the liquid-phase concentrations of solutes at the initial time and at equilibrium, respectively, v (L) is the volume of solution and w the mass of resin (g). Ion exchange rates were determined at the desired pH and temperature in an orbital shaker.…”

Section: Experimental Methodsmentioning

confidence: 99%

“…A cation resin can easily take up an amino acid at a pH value in which the amino acid is positively charged and can desorb it when the amino acid is negatively charged. The characteristics of adsorption behavior are generally inferred in terms of the equilibrium isotherm, adsorption kinetics and thermodynamics, with which a rational design and optimization of such ion exchange processes can be constructed [7][8][9]. In this study, seven cation resins were screened to obtain the most suitable resin for Ltrp separation.…”

Section: Introductionmentioning

confidence: 99%

Adsorption behavior of L-tryptophan on ion exchange resin

Wei

Chen

Fan

et al. 2011

Korean J. Chem. Eng.

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A batch method was applied to investigate the adsorption behavior and mechanisms of L-tryptophan (Ltrp) on ion exchange resins. HZ-001 and JK006 were proved to be ideal adsorbents due to their large loading capacity and favorable selective adsorption for L-trp. Langmuir, Freundlich, and Dubinin-Radushkevich equations were applied to simulate the experimental data to describe the adsorption process of L-trp onto HZ-001 and JK006. The maximum loading capacity (at pH 5.0, 30 o C), determined by the Langmuir and Dubinin-Radushkevich models, was close to each other (833 mg/g vs. 874 mg/g) for HZ-001, while discrepant (833 mg/g vs. 935 mg/g) for JK006. Three diffusion-controlled kinetic models were utilized to analyze the results in order to identify the adsorption mechanism. The adsorption kinetics of L-trp onto cation exchange resins was investigated under different experimental conditions, including initial solution pH, temperature, initial L-trp concentration, and adsorbent dosage. Moreover, the diffusion process of L-trp onto HZ-001 and JK006 was evaluated at different initial adsorbate concentrations. The thermodynamic parameters, obtained from the kinetic data, demonstrated that L-trp could be adsorbed spontaneously onto both resins.

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“…To evaluate the ability of PCB-PAC to isolate molecules bound to plasma proteins, bilirubin-albumin (BR-BSA) solution was prepared by dissolving solid bilirubin in 0.1 M NaOH, then adding the resulting solution into BSA solution, and the final pH was adjusted to 7.4 [38]. PCB-PAC particles (containing 30 mg PAC for each test) were placed into flasks containing 5 mL BR-BSA solution (150 mg/L BR, 40 mg/mL BSA).…”

Section: Adsorption Of Bilirubin From Albuminmentioning

confidence: 99%