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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↗
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↗
PubMed2001

Comparison of chromatographic ion-exchange resins. II. More strong anion-exchange resins.

A comparative study was performed on strong anion exchangers to investigate the pH dependence, titration curves, efficiency, binding strength, particle size distribution, and static and dynamic capacity of the chromatographic resins. The resins tested included Q Sepharose XL, UNO Q-1, Poros 50 HQ, Toyopearl QAE 550c, Separon HemaBio 1000Q, Q-Cellthru Bigbeads Plus, Q Sepharose HP and Toyopearl SuperQ 650s. Testing was performed with five different proteins: anti-Factor VII monoclonal antibody (immunoglobulin G), aprotinin, bovine serum albumin, lipolase and myoglobin. The dependence of pH on retention varies from generally low to very high for proteins with a low isoelectric point (pl). An unexpected binding at pH 7-8 of aprotinin with pI >11 was observed on Separon HemaBio 1000Q. No link between pH dependence on retention and titration curves of the different resins was observed. 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. No or a very small difference in particle size distribution was obtained between new and used resins. Binding to anion-exchange resins as a function of ionic strength varies to some extent depending on the specific protein. Generally, binding and elution at high salt concentration may be performed with Q Sepharose XL, Toyopearl QAE 550c, Q Sepharose HP and Poros 50 HQ, while binding and elution at low salt concentration may be performed with Q-Cellthru Bigbeads Plus. A very high binding capacity was obtained with Q Sepharose XL. Comparison of static capacity and dynamic capacity at 10% breakthrough shows approx. 50-80% utilization of the total available capacity during chromatographic operation. A general good agreement was obtained between this study and data obtained by the suppliers. The results of this study may be used for selection of resins for testing in process development.

Anion Exchange Resins↗
PubMed1983

Preparation of a biocompatible albumin-coated ion exchange resin for bilirubin removal from the blood of jaundiced newborns.

Removal of bilirubin by hemoperfusion with ion exchange resin particles is suggested to replace exchange transfusion of blood of jaundiced infants in some cases of unconjugated hyperbilirubinemia. The hemoperfusion system developed here consists of a packed bed of a macroreticular resin which is made biocompatible by a coating of a monomolecular layer of albumin. The choice of the appropriate ionic form of the resin and the proper albumin coating and crosslinking procedure assures a high bilirubin adsorption capacity and excellent blood compatibility of the resin. The albumin coated resin removes in vitro 80-90% of the bilirubin initially present in the plasma. The results encourage in vivo clinical studies.

Adsorption↗
PubMed1971

Biological ion exchanger resins. I. Quantitative electrostatic correspondence of fixed charge and mobile counter ion.

Utilizing Escherichia coli as the prototype of an ion-accumulating cell, the ion exchange isotherm is introduced as a concise method of characterizing biological ion exchange events. The ion exchange isotherm for the alkali cation exchange, K <--> Na, is described. The total charge profile of this bacterium is compiled and compared for bacteria in the Na form and in the K form. Macromolecule fixed charge was found to provide 80% of the counter ions that pair with potassium. Therefore, in its physiological state, 80% of the cell potassium in E. coli is associated with an ion exchange site on a macromolecule. The primary cation exchange sites are found to be about equally divided between carboxylate and phosphate sites indicating that E. coli is a bifunctional resin with respect to cation exchange. During substrate-dependent cation accumulation ("active transport"), phosphate esters and organic acids were shown to accumulate. One may conclude that the role of intermediate metabolism in "active transport" is to increase the ion exchange capacity of the biological resin by the production of charged metabolites that sorb to the framework of the resin.

Amines↗
PubMed2005

Suspensions of prolonged-release diclofenac-Eudragit and ion-exchange resin microcapsules: II. Improved dissolution stability.

PURPOSE: The stability of prolonged release 100 microm -size ion-exchange resin (IER) diclofenac microcapsules (prepared by the Wurster process) and coated with Eudragit RS30D was evaluated using dissolution analysis. METHODS: The IER microcapsules were suspended in 0.1% methylcellulose and stored at 23 and 37 degrees C and the dissolution study conducted over a 6-month period. The surface morphology of the microcapsules was examined using scanning electron microscopy (SEM). RESULTS: The dissolution of the suspensions stored at 23 degrees C on day 1 or 7 and was similar to that of day 30 with slightly faster dissolution on day 60. In contrast, release from suspensions stored at 37 degrees C decreased with storage. The decrease in dissolution with increased temperature was possibly due to the polymer relaxation (micromelting) that was enough to seal the drug within the matrix, resulting in slow dissolution. SEM of the suspended microcapsules correlated with the dissolution data, i.e. the surfaces of microcapsule stored at 37 degrees C showed decreased roughness or smoothening and closing of pores with time and, hence, retardation of drug release, compared with samples stored at 23 degrees C. The dissolution kinetics (shown by the linearity of Bt vs. time profiles) indicated that release mechanism was diffusion. CONCLUSIONS: The suspensions of diclofenac IER microcapsules were stable up to 30 days at ambient temperature, which makes the formulation potentially useful as reconstitutable product.

Acrylic Resins↗
PubMed2005

Improved and selective platinum recovery from spent alpha-alumina supported catalysts using pretreated anionic ion exchange resin.

Improved and selective recovery of platinum from a spent dehydrogenation platinum alpha-alumina supported catalyst using a strong basic ion exchange resin is reported. Platinum and other precious metal group (PMG) complexes are leached using concentrated hydrochloric acid along with about 0.20 vol.% nitric acid as an oxidizing agent from de-coked and crushed spent catalyst. Effects of hydrochloric acid concentration, time, and temperature in leaching stage are investigated. The strong basic anionic resin is treated by sodium hydroxide solution to replace chloride anion by hydroxyl group ion. The supernatant of the leaching process is passed through a fixed column of hydroxylated strong base anionic resin. The treated resin on which the platinum complex is adsorbed is dried and burned in an oxidizing atmosphere at 750-800 degrees C. The recovered gray metallic powder is mainly platinum. Results compared with those obtained from untreated anionic resin show that adsorption of platinum complexes onto the treated anionic resin is more selective and the yield of separation is considerably improved. The breakthrough curves of the pretreated anion exchanger and that of untreated exchange resin reveals that the capacity of the hyroxilated resin is decreased by about 14%. These breakthrough curves can be used for calculation of height of a practical exchange plate (HPEP) for design purposes.

Aluminum Oxide↗
PubMed2004

Cleaning power and abrasivity of a new toothpaste based on ion-exchange resins.

PURPOSE: To compare the stain removal efficacy and enamel abrasivity of a new experimental dentifrice based on an ion-exchange resin mixture that releases calcium, fluoride, phosphate and zinc ions (named NMTD1), to four commercially available dentifrices: Crest Extra-whitening toothpaste, Crest Tartar Protection toothpaste, Crest Cavity Protection toothpaste and Colgate Fluoride Cavity Protection toothpaste. Calcium pyrophosphate was used as a control for the efficacy of the staining removal experiment. METHODS: Cleaning power evaluation was made following the method developed by Stookey et al. The abrasion of the toothpastes was determined by means of a brushing machine, using 2000, 4000 and 8000 strokes and a 250g toothbrush load. Bovine specimens were prepared and abrasion was measured by a surface profilometer system. RESULTS: The new experimental dentifrice did not remove stains whereas Crest Extra-whitening and Crest Cavity Protection dentifrices produced statistically significant stain removal when compared with the calcium pyrophosphate control. Abrasion studies demonstrated that abrasion was linearly correlated to the number of strokes and the abrasion rates proved to be non significant for Colgate and the new experimental dentifrices, but significant for Crest Extra-whitening, Crest Tartar Protection and Crest Cavity Protection. CLINICAL SIGNIFICANCE: This study demonstrated that the use of a dentifrice based on an ion-exchange mixture was not effective at removing stains and abrasion was most insignificant when compared to other commercially available toothpastes.

Animals↗
PubMed1977

Nuclear magnetic resonance chemical shifts of potassium ions (39K) on ion exchange resins and in muscle.

Chemical shifts of potassium (39K) were calculated from frequencies of beat patterns measured by a pulsed NMR method. This method indicates large chemical shifts for 3 molar KNO3 and 6 molal KI in good quantitative agreement with the steady state NMR measurements of previous investigators. 39K on two wet ion exchange resins and 39K in fresh muscle show insignificant chemical shifts relative to 0.1 M KCl solution. Previous studies showed marked shortening of NMR relaxation times (T1 and T2) for 39K in ion exchange resins and in muscle compared to free solution. These results seem to indicate that even though potassium on resins and in muscle experiences high electric field gradients, these have relatively little effect on the chemical shift of potassium, which may be correlated with the low pK values of the anionic groups in the resins and muscle.

Animals↗