[New type of ion exchange demineralizer].
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The interactions between ion-exchange resins and counterions consist of several mechanisms, such as ion-pair formation between active sites and counterions, specific adsorption, solvation changes, and double-layer accumulation. The double-layer accumulation of ions, which is a typical nonstoichiometric mechanism, is an important factor governing overall ion-exchange chromatographic retention when a major part of the stationary-phase surface is in contact with eluent flows. Nonporous stationary phases, where solutes are accessible to the surfaces by convection as well as by diffusion, possibly highlight this nonstoichiometric contribution through the coupling of a flow profile with an electrostatic potential function. The retention of ions on nonporous stationary phases has been interpreted by a model derived on the basis of the Poisson-Boltzmann equation including solvation change terms. Unusual retention behaviors have been confirmed only for anions, and can be explained by the model including the assumption that anions undergo solvation changes in a thin layer (approximately 5 nm thickness) at the vicinity of the stationary phase; the thickness should be a function of eluent flow rates. This strongly suggests that there is a difference in solvation nature between cations and anions. It can be inferred that water molecules interacting with polymer domains of the stationary phase behave like single molecules and cannot form a stable hydration shell around an anion as usually seen in bulk solution.
A combined gas chromatographic-mass spectrometric technique is described for the quantification of virazole in serum and urine. Proteins are removed by molecular filtration, lipids by extraction with dichloromethane and interfering endogenous constituents by acidic and basic ion-exchange resins. Virazole is quantified by monitoring the protonated molecular ions of the fully silylated derivatives of virazole (m/e 533) and the arabinose analog (internal standard) obtained by methane chemical ionization. The detection limit is 150 pg (0.6.10(-12) mole) of virazole injected. In serum 10 ng/ml (4.10(-8) mole) can be detected, 25 ng/ml quantified. In urine 0.5 microgram/ml can be quantified without preconcentration. Virazole was detected in serum for at least 96 h at the 70-ng/ml level.
The use of sorbents in different blood purification techniques is reviewed. The sorbents used in these therapies are divided into two groups: (1) Adsorption occurs fundamentally because of the hydrophobic properties of the sorbents. In this group, the sorbents used in different dialysis techniques are charcoal and nonionic macroporous resins. (2) Adsorption occurs by chemical affinity, such as ion exchange resins and chemisorbents. Sorbents were initially used in hemoperfusion, which caused many adverse events; later, with the use of coated charcoal, these undesired effects decreased or disappeared, but the adsorptive properties, water control, and acid-base balance still created problems. For these reasons, the use of sorbents in the treatment of chronic renal failure was almost totally discontinued. Little by little, interest in these substances has reappeared, and at present, they have been used in combination with other blood purification techniques such as hemodialysis, hemofiltration, peritoneal dialysis, and finally, hemodiafiltration. Within the various hemodiafiltration techniques, paired filtration dialysis-charcoal is being used to regenerate the ultrafiltrate, which is used as the replacement fluid. Charcoal regenerates the ultrafiltrate and transforms it into a physiological solution with a normal electrolyte composition, calcium, bicarbonate, and glucose, having eliminated the majority of both middle and large molecule uremic toxins. If regeneration is done properly, this replacement fluid is bacteria and endotoxin free. Studies currently are underway on the adsorption of different inflammatory substances in the ultrafiltrate, which could lead to improvement in the biocompatibility of the system.
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The applicability of the stoichiometric displacement model (SDM) to description of the retention behavior of charged-fusion proteins in large ion exchange resin (approximately 90 microm diameter) packed column was studied. Proteins were characterized by SDM for isocratic elution. The parameters were subsequently used to evaluate their suitability in predicting protein retention and peak width under gradient elution. The proteins were beta-glucuronidase (GUS) and its fusions with polypeptides of 5, 10 and 15 aspartic acids at the C-terminal of the wild-type GUS. Predictions of retention time were within 10% of the experiment results. The plate number obtained at high salt concentration from isocratic elution was used as a first estimate for predictions of peak width. The results show that the SDM is sufficient to describe the binding equilibrium of fusion proteins in ion-exchange columns packed with large resin particles. In addition, the binding mechanism between fusion proteins and the ion exchanger is explored with the assistance of comparative molecular modeling.
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