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PubMed1984

Effects of azotemia on results of the boronate-agarose affinity and ion-exchange methods for glycated hemoglobin.

We evaluated the effect of azotemia on results for glycated hemoglobin as measured by a boronate-agarose affinity method and an ion-exchange chromatographic procedure with saline preincubation and found a good correlation. However, values for glycated hemoglobin in samples from nondiabetic patients with various degrees of azotemia were consistently higher with the ion-exchange column procedure (mean, 8.5%) than with the boronate affinity method (mean, 6.2%). The latter method may thus be preferred for monitoring glycated hemoglobin in diabetic patients with impaired renal function.

Boronic Acids↗
PubMed1997

Characteristics of the adsorption of immunoglobulin M onto Q Sepharose Fast Flow ion-exchangers.

Measurement of adsorption breakthrough curves in packed beds has shown that the amounts and rates of uptake of immunoglobulin M (IgM) onto the commonly used anionic ion-exchanger Q Sepharose Fast Flow (based on 6% agarose) are severely limited as a result of the large molecular size of this adsorbate (RMM 950,000). A similar ion-exchanger based on a more porous 4% agarose, Q Sepharose 4 Fast Flow was evaluated as an alternative adsorbent for the purification of IgM. Equilibrium adsorption isotherms and the effective diffusivities of IgM within these two adsorbents were measured. Q-Sepharose 4 Fast Flow was found to have a maximum capacity for IgM 2.5 times greater than that of Q Sepharose 6 Fast Flow and the effective diffusivity of IgM was found to be between 6 and 7 times greater than with the latter material. Comparison of the breakthrough curves obtained for these adsorbents at a variety of flow velocities confirm that Q Sepharose 4 Fast Flow is a superior adsorbent for the capture and purification of large proteins.

Adsorption↗
PubMed1993

Human IgG preparations isolated by ion-exchange or protein G affinity chromatography differ in their glycosylation profiles.

IgG from patients with rheumatoid arthritis (RA) is abnormally glycosylated in the Fc region, with sialic acid and galactose levels lower than normal. Protein G and DEAE purify populations which are differentially glycosylated. Significantly increased exposure of sialic acid was detected in normal IgG compared with that of RA IgG when ion exchange was used to prepare samples. However, when the same samples were prepared using protein G, no difference in the detection of sialic acid was seen between the two groups. When examining the heavy chain of IgG, more sialic acid, galactose and N-acetylglucosamine were detected in DEAE purified IgG compared with that prepared by protein G Detection of sialic acid and N-acetylglucosamine was also increased on light chains from IgG prepared by ion exchange chromatography. Since this occurs notably on rheumatoid light chains it would appear that this arrangement would contribute to the overall glycosylation changes in IgG. In the case of molecules lacking galactose the discrimination between the RA and normal IgG is significantly improved when ion exchange chromatography is used. Since differentiation between disease and normal groups relies on the purification technique used, we recommend that more than one method is employed before undertaking an analysis of glycosylation changes.

Arthritis, Rheumatoid↗
PubMed1984

Separation of choline- and ethanolamine-labeled metabolites by ion-exchange high-pressure liquid chromatography.

Two methods utilizing ion-exchange high-performance liquid chromatography have been developed for the separation of choline- and ethanolamine-containing metabolic precursors for phosphatidylcholine and phosphatidylethanolamine. Both methods employ an analytical anion-exchange column supplemented with a cation-exchange column; the latter is required only to separate betaine from choline. Complete separation of choline- and ethanolamine-labeled metabolites from extracts of Chinese hamster ovary cells can be achieved in 20 min.

Animals↗
PubMedDate not supplied

[Ion exchange resins].

Explore the source record for details and available documents.

Ion Exchange Resins↗
PubMed2004

Thermodynamic clarification of the curious ferric/potassium ion exchange accompanying the electrochromic redox reactions of prussian blue, iron(III) hexacyanoferrate(II).

The recent Glasser-Jenkins method for lattice-energy prediction, applied to an examination of the solid-state thermodynamics of the cation exchanges that occur in electrochromic reactions of Prussian Blue, provides incisive thermodynamic clarification of an ill-understood ion exchange that accompanies particularly the early electrochromic cycles. A volume of 0.246 +/- 0.017 nm(3) formula unit(-1) for the ferrocyanide ion, Fe(II)[(CN)(6)],(4-) is first established and then used, together with other formula unit-volume data, to evaluate the changes of standard enthalpy, entropy, and Gibbs energy in those ion-exchange reactions. The results impressively show by how much the exchange of interstitial Fe(3+) ions by alkali metal ions, usually exemplified by K+, is thermodynamically favored.

Journal Article↗
PubMed2000

Improvement purification of sulfated oligofucan by ion-exchange displacement centrifugal partition chromatography.

Centrifugal partition chromatography in ion-exchange displacement mode was used to fractionate mixtures of sulfated oligofucans obtained by partial depolymerization of brown seaweed fucoidans. Diluted (10%, v/v) protonated LA2 (a lipophilic secondary amine) is used as a weak exchanger. In an attempt to improve this method, several solvents (methyl isobutyl ketone, methyl tert.-butyl ether, BuOH) were tested to dissolve LA2H+. MtBE produced less bleeding than MiBK, whereas BuOH proved unsuitable. The sample injected needs to be highly diluted in water to ensure participation in the chromatographic process. A comparison of data (NMR, composition, molecular mass) indicated the homogeneity of the fractions obtained as well as the differences between them.

Centrifugation↗
PubMed2001

Computer simulation of ion chromatography separation: an algorithm enabling continuous monitoring of anion distribution on an ion-exchange chromatography column.

A computer algorithm for the calculation of ion chromatography separation is presented. It is based on the calculation of equilibrium concentrations of present analyte in discrete column segments. The continuous column is treated as a number of discrete cells or segments where the equilibration process between the stationary phase and the eluent is simulated. The ion-exchange equilibration process is supposed to be instantaneous and quantitative. The continuous flow of the eluent is rendered by discrete transfers. The size of each transfer of the eluent corresponds to a portion of the volume contained in one column segment. The equilibrium calculations in all column segments are repeated for each transfer of the eluent, through all the stages of the chromatographic process. The distribution of the analytes between the stationary phase and the eluent can be monitored at any step and in any column segment which means that the described algorithm provides the spatial and time concentration profiles. The simulated chromatogram is acquired as a time-concentration profile in the last column segment. The obtained chromatograms are in good agreement with the experimental ones. The distribution of ions between the stationary phase and the eluent in the early stages of the ion chromatographic process can thus be studied with confidence.

Algorithms↗