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CATION-EXCHANGE resins.

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Cation Exchange Resins↗
PubMed2004

Comparison of chromatographic ion-exchange resins. III. Strong cation-exchange resins.

A comparative study was performed on strong cation-exchangers to investigate the pH dependence, efficiency, binding strength, particle size distribution, static and dynamic capacity, and SEM pictures of chromatographic resins. The resins tested included: SP Sepharose XL, Poros 50 HS, Toyopearl SP 550c, SP Sepharose BB, Source 30S, TSKGel SP-5PW-HR20, and Toyopearl SP 650c. Testing was performed with four different proteins: anti-FVII Mab (IgG), aprotinin, lysozyme, and myoglobin. Dependence of pH on retention was generally very low for proteins with high pI. An unexpected binding at pH 7.5 of anti-FVII Mab with pI < 7.5 was observed on several resins. Efficiency results show the expected trend of higher dependence of the plate height with increasing flow rate of soft resins compared to resins for medium and high-pressure operation. Determination of particle size distribution by two independent methods, Coulter counting and SEM, was in very good agreement. The mono-dispersed nature of Source 30S was confirmed. Binding to cation-exchange resins as a function of ionic strength varies depending on the specific protein. Generally, binding and elution at high salt concentration may be performed with Toyopearl SP 550c and Poros 50 HS, while binding and elution at low salt concentration may be performed with Toyopearl SP 650c. A very high binding capacity was obtained with SP Sepharose XL. Comparison of static capacity and dynamic capacity at 10% break-through shows in general approximately 50-80% utilisation of the total available capacity during chromatographic operation. A general good agreement was obtained between this study and data obtained by others. The results of this study may be used for selection of resins for testing in process development. The validity of experiments and results with model proteins were tested using human insulin precursor in pure state and in real feed-stock on Toyopearl SP 550c, SP Sepharose BB, and Toyopearl SP 650c. Results showed good agreement with experiments with model proteins.

Cation Exchange Resins↗
PubMed2003

[Study on the defluoridation of drinking water with model-La cation exchange resin].

Model-La cation exchange resin was transformed from strong acid cation exchange resin, which was used for the defluoridation of drinking water. The 001 x 7 strong acid cation exchange resin was transformed into model-La cation exchange by soaking in the La(NO3)3 solution. The F- in the water was removed by model-La cation exchange resin under the optimum condition because it was combined into fluoride with the La3+ in the model-La cation exchange resin. The used resin was regenerated with the La(NO3)3 solution and was used to defluoridate many times. The optimum conditions of transform and defluoridation and regeneration were d(rasin) = 0.315-0.600 mm, V(rasin):V(regeneration) = 1:6, t(transform) = 48 h, T = 298.16 K(25 degrees C). The defluoridation capacity was 5.60 mg/g in column test, and 4.08 mg/g in batch test. The model-La cation exchange resin could be used for defluoridation for 8 times. The results suggest that the model-La cation exchange resin is a novel material of defluoridation. This method is easy to master and the pH value of the solution doesn't need to be regenerated that the cost of defluoridation can be reduced significantly and it can be used for a long time.

Cation Exchange Resins↗
PubMed2006

Comparison of chromatographic ion-exchange resins V. Strong and weak cation-exchange resins.

Strong and weak cation-exchangers were compared for a number of chromatographic parameters, i.e. pH dependence, efficiency, binding strength, particle size distribution, static and dynamic capacity, and scanning electron microscopy (SEM) pictures. Chromatographic resins investigated were Fractogel EMD SO3- (M), Fractogel EMD SE Hicap (M), Fractogel EMD COO- (M), MacroPrep 25S, MacroPrep High S, MacroPrep CM, CM HyperZ, and Matrex Cellufine C-500. Testing was done with three proteins: Anti-FVII Mab (IgG), aprotinin, and lysozyme. For lysozyme and aprotinin with pI above experimental pH, dependence of pH on retention was generally low, though some pronounced decrease of retention with increasing pH was observed for CM HyperZ. For Anti-FVII Mab with pI<7.5, binding was observed on several resins at pH 7.5. Efficiency results present the expected trend of increasing dependence of plate height as a function of increasing flow rate, and the highest flow dependence was observed for Fractogel EMD COO-. Particle size distribution was determined by two independent methods, coulter counting and SEM pictures, with fair agreement. Binding strength data of cation-exchange resins as a function of ionic strength depends on the protein, but binding and elution at high salt concentration may in general be performed with MacroPrep resins. Comparison of dynamic capacity data at 10% break-through and static capacity measurements shows that a very diverse utilization of approximately 25-90% of the total available capacity is employed during chromatographic operation. The effect of competitive binding from yeast fermentation components on dynamic binding capacity of aprotinin was studied showing a significant decrease in binding capacity. Sepharose FF, Toyopearl 650 M, and Ceramic HyperD F strong and weak cation-exchange resins were included in this study. Resins with good pure aprotinin capacity also performed well for aprotinin in fermentation broth, but the highest relative capacity was obtained with MacroPrep High S having a fairly low pure component dynamic capacity. Results of this paper may be used in the selection of resins for further testing in biopharmaceutical protein purification process development.

Cation Exchange Resins↗
PubMed2005

Comparison of chromatographic ion-exchange resins IV. Strong and weak cation-exchange resins and heparin resins.

A comparative study was performed on heparin resins and strong and weak cation exchangers to investigate the pH dependence, efficiency, binding strength, particle size distribution, static and dynamic capacity, and scanning electron microscopy pictures of chromatographic resins. The resins tested include: Heparin Sepharose FF, SP Sepharose FF, CM Sepharose FF, Heparin Toyopearl 650 m, SP Toyopearl 650 m, CM Toyopearl 650 m, Ceramic Heparin HyperD M, Ceramic S HyperD 20, and Ceramic CM HyperD F. Testing was performed with four different proteins: anti-FVII Mab (IgG), aprotinin, lysozyme, and myoglobin. Dependence of pH on retention was generally very low for proteins with high isoelectric point (pI), though some decrease of retention with increasing pH was observed for CM Ceramic HyperD F and S Ceramic HyperD 20. Binding of anti-FVII Mab with pI < 7.5 was observed on several resins at pH 7.5. Efficiency results show the expected trend of increasing dependence of the plate height with increasing flow rate of Ceramic HyperD resins followed by Toyopearl 650 m resins and the highest flow dependence of the Sepharose FF resins corresponding to their pressure resistance. Determination of particle size distribution by two independent methods, coulter counting and SEM, was in good agreement. Binding strength of cation-exchange resins as a function of ionic strength varies depending on the protein. Binding and elution at high salt concentration may be performed with Ceramic HyperD resins, while binding and elution at low salt concentration may be performed with model proteins on heparin resins. Employing proteins with specific affinity for heparin, a much stronger binding is observed, however, some cation exchangers may still be good substitutions for heparin resins. Dynamic capacity at 10% breakthrough compared to static capacity measurements and dynamic capacity displays that approximately 40-80% of the total available capacity is utilized during chromatographic operation depending on flow rate. A general good agreement was obtained between results of this study and data obtained by others. Results of this study may be used in the selection of resins for testing during protein purification process development.

Cation Exchange Resins↗
PubMed1985

Cation-induced histamine release from a synthetic weak (carboxylic) cation exchanger resin (IRC-50) and from isolated mast cell granules show identical kinetics.

Comparative studies between synthetic weak cation exchanger resins and rat mast cell granules have shown that the cation-induced release of histamine from both materials follows the kinetics characteristic of cation exchange. Since also cation-induced release of amines from chromaffin granules in vitro and chromaffin cells in vivo, as also nerve granules of peripheral and central neurons, run according to cation exchange kinetics, cation exchange might be a general principle in the storage and release of biogenic amines.

Animals↗
PubMed2002

Studies on adsorptive removal of Co(II), Cr(III) and Ni(II) by IRN77 cation-exchange resin.

The adsorption of cobalt, chromium and nickel from aqueous solutions on IRN77 cation-exchange resin has been studied comparatively. The percentage removal of cobalt, chromium and nickel was examined by varying experimental conditions, viz. dosage of adsorbent, pH of the solution and contact time. It was found that more than 95% removal was achieved under optimal conditions. The adsorption capacity (k) for cobalt, chromium and nickel were calculated from the Freundlich adsorption isotherm. The adsorption of cobalt, chromium and nickel on this cation-exchange resin followed the Lagergren kinetic model. Also the competitive adsorption of multi-metals onto the IRN77 resin was studied. The studies showed that this cation-exchange resin can be used as an efficient adsorbent material for the removal of cobalt, chromium and nickel from water and nuclear power plant coolant water.

Adsorption↗