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Journal articles on the topic 'Ion exchange chromatography'

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Published: 4 June 2021
Last updated: 30 July 2024

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1

Ghatak-Roy, Amiya R., and Charles R. Martin. "Electromodulated ion exchange chromatography." Analytical Chemistry 58, no. 7 (June 1986): 1574–75. http://dx.doi.org/10.1021/ac00298a070.

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2

Sellergren, Börje, and Kenneth J. Shea. "Chiral ion-exchange chromatography." Journal of Chromatography A 654, no. 1 (November 1993): 17–28. http://dx.doi.org/10.1016/0021-9673(93)83061-v.

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3

SHIBUKAWA, Masami, Ryota MORINAGA, and Shingo SAITO. "Superheated Water Ion-exchange Chromatography." Bunseki kagaku 65, no. 11 (2016): 615–23. http://dx.doi.org/10.2116/bunsekikagaku.65.615.

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4

Milby, Kristin H., Sa V. Ho, and Jay M. S. Henis. "Ion-exchange chromatography of proteins." Journal of Chromatography A 482, no. 1 (January 1989): 133–44. http://dx.doi.org/10.1016/s0021-9673(01)93214-5.

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5

Sarwar, Ghulam, Herbert G. Botting, and Robert W. Peace. "Complete Amino Acid Analysis in Hydrolysates of Foods and Feces by Liquid Chromatography of Precolumn Phenylisothiocyanate Derivatives." Journal of AOAC INTERNATIONAL 71, no. 6 (November 1, 1988): 1172–75. http://dx.doi.org/10.1093/jaoac/71.6.1172.

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Abstract The amino acid analysis method using precolumn phenylisothiocyanate (PITC) derivatization and liquid chromatography was modified for accurate determination of methionine (as methionine sulfone), cysteine/cystine (as cysteic acid), and all other amino acids, except tryptophan, in hydrolyzed samples of foods and feces. A simple liquid chromatographic method (requiring no derivatization) for the determination of tryptophan in alkaline hydrolysates of foods and feces was also developed. Separation of all amino acids by liquid chromatography was completed in 12 min compared with 60-90 min by ion-exchange chromatography. Variation expressed as coefficients of variation (CV) for the determination of most amino acids in the food and feces samples was not more than 4%, which compared favorably with the reproducibility of ion-exchange methods. Data for amino acids and recoveries of amino acid nitrogen obtained by liquid chromatographic methods were also similar to those obtained by conventional ion-exchange procedures.
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6

Kato, Yoshio, Shigeru Nakatani, Takashi Kitamura, Akane Onaka, and Tsutomu Hashimoto. "High-performance ion-exchange chromatography of peptides on a pellicular ion exchanger." Journal of Chromatography A 513 (January 1990): 384–88. http://dx.doi.org/10.1016/s0021-9673(01)89461-9.

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7

Cooper, J. D. H., D. C. Turnell, B. Green, D. J. Wright, and E. J. Coombes. "Why the Assay of Serum Cystine by Protein Precipitation and Chromatography Should Be Abandoned." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 25, no. 5 (September 1988): 577–82. http://dx.doi.org/10.1177/000456328802500516.

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The higher bias of serum cystine estimations by a HPLC method compared with those by ion exchange techniques is shown to be largely due to differences in the sample preparation procedures of the two techniques. The ion exchange methods utilised sulphosalicylic acid serum protein precipitation and post-column ninhydrin derivatisation of cystine, whilst the high pressure liquid chromatography technique employed automated dialysis for removal of proteins and pre-column ortho-phthalaldehyde derivatisation of cystine after its conversion to cysteine and then to S-carboxymethylcysteine. Examination of these procedures showed that whilst the high pressure liquid chromatographic method accurately estimates total serum cystine and cysteine, many factors affect the precision and accuracy of serum cystine estimations using the ion exchange techniques. In particular, serum protein precipitation techniques that are currently employed for the preparation of samples for cystine analysis by ion exchange chromatography should be abandoned.
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8

Schmuckler, Gabriella. "High-Performance Liquid Ion-Exchange Chromatography." Journal of Liquid Chromatography 10, no. 8-9 (June 1987): 1887–901. http://dx.doi.org/10.1080/01483918708066804.

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9

Lettner, H. P., O. Kaltenbrunner, and A. Jungbauer. "HETP in Process Ion-Exchange Chromatography." Journal of Chromatographic Science 33, no. 8 (August 1, 1995): 451–57. http://dx.doi.org/10.1093/chromsci/33.8.451.

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10

Nakamura, Koji, and Yoshio Kato. "Preparative high-performance ion-exchange chromatography." Journal of Chromatography A 333 (January 1985): 29–40. http://dx.doi.org/10.1016/s0021-9673(01)87322-2.

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11

Okada, Tetsuo. "Nonaqueous ion-exchange chromatography and electrophoresis." Journal of Chromatography A 804, no. 1-2 (April 1998): 17–28. http://dx.doi.org/10.1016/s0021-9673(97)01234-x.

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12

Jayaraman, Guhan, Shishir D. Gadam, and Steven M. Cramer. "Ion-exchange displacement chromatography of proteins." Journal of Chromatography A 630, no. 1-2 (February 1993): 53–68. http://dx.doi.org/10.1016/0021-9673(93)80441-a.

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13

Araujo, B. F., H. T. Matsuda, E. I. Carvalho, and I. C. Araujo. "Plutonium removal by ion exchange chromatography." Journal of Radioanalytical and Nuclear Chemistry Letters 165, no. 4 (July 1992): 209–17. http://dx.doi.org/10.1007/bf02164760.

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14

Ljunglöf, Anders, Karol M. Lacki, Jay Mueller, Chithkala Harinarayan, Robert van Reis, Robert Fahrner, and James M. Van Alstine. "Ion exchange chromatography of antibody fragments." Biotechnology and Bioengineering 96, no. 3 (2006): 515–24. http://dx.doi.org/10.1002/bit.21124.

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15

Small, Hamish, and John Riviello. "Electrically Polarized Ion-Exchange Beds in Ion Chromatography: Ion Reflux." Analytical Chemistry 70, no. 11 (June 1998): 2205–12. http://dx.doi.org/10.1021/ac980075+.

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16

Dasgupta, Purnendu K., and Fereshteh Maleki. "Ion exchange membranes in ion chromatography and related applications." Talanta 204 (November 2019): 89–137. http://dx.doi.org/10.1016/j.talanta.2019.05.077.

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17

Pohl, Christopher A., John R. Stillian, and Peter E. Jackson. "Factors controlling ion-exchange selectivity in suppressed ion chromatography." Journal of Chromatography A 789, no. 1-2 (November 1997): 29–41. http://dx.doi.org/10.1016/s0021-9673(97)00705-x.

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18

Carling, Rachel S., Benjamin AC McDonald, Donna Austin, Deborah Burden, Joana Correia, Jenny Leung, Beverley Mayers, and Catharine John. "Challenging the status quo: A comparison of ion exchange chromatography with liquid chromatography–mass spectrometry and liquid chromatography–tandem mass spectrometry methods for the measurement of amino acids in human plasma." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 57, no. 4 (July 2020): 277–90. http://dx.doi.org/10.1177/0004563220933303.

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Background Plasma amino acid analysis is key to the diagnosis and monitoring of inherited disorders of amino acid synthesis, catabolism and transport. Ion exchange chromatography (IEC) is widely accepted as the gold standard method of analysis, but with the introduction of liquid chromatography tandem mass spectrometry (LC-MS/MS) and liquid chromatography mass spectrometry (LC-MS) methods, this should now be questioned. Methods The analytical performance of three commercially available reagent kits, Waters AccQ Tag™ ULTRA LC-MS, SpOtOn Amino Acids LC-MS/MS and Chromsystems MassChrom® Amino Acid Analysis LC-MS/MS, were evaluated and compared with Biochrom Physiological Amino Acids ion exchange chromatography. Correlation with IEC was assessed by Passing-Bablok regression, concordance correlation coefficients (CCC) and Bland-Altman analysis for 21 common amino acids. Calculation of the total error from imprecision and bias was also used to benchmark performance. Results The MassChrom® and SpOtOn kits demonstrated acceptable inter-batch imprecision (CV < 10%) and accuracy (mean bias < 10%), whereas the AccQ Tag™ ULTRA kit did not. Good correlation (CCC > 0.95) with Biochrom IEC was demonstrated for 10/21 analytes in both the MassChrom® and SpOtOn kits and 6/21 in the AccQ Tag™ ULTRA kit. Conclusions The LC-MS assay demonstrated variable analytical performance and correlated poorly with ion exchange chromatography. Both LC-MS/MS assays demonstrated comparable analytical performance and reasonable correlation with ion exchange chromatography. They also confer practical advantages which cannot be realized by ion exchange chromatography, superior specificity and significantly faster analysis time, suggesting that ion exchange chromatography should no longer be described as the gold standard method for plasma amino acid analysis.
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19

Kaine, Lisa A., John B. Crowe, and Karen A. Wolnik. "Forensic applications of coupling non-suppressed ion-exchange chromatography with ion-exclusion chromatography." Journal of Chromatography A 602, no. 1-2 (June 1992): 141–47. http://dx.doi.org/10.1016/0021-9673(92)80074-5.

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20

Branthaver, J. F., M. W. Catalfomo, and J. C. Petersen. "ION EXCHANGE CHROMATOGRAPHY SEPARATION OF SHRP ASPHALTS." Fuel Science and Technology International 10, no. 4-6 (January 1992): 855–85. http://dx.doi.org/10.1080/08843759208916025.

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21

Schols, H. A., J. C. E. Reitsma, A. G. J. Voragen, and W. Pilnik. "High-performance ion exchange chromatography of pectins." Food Hydrocolloids 3, no. 2 (April 1989): 115–21. http://dx.doi.org/10.1016/s0268-005x(89)80021-9.

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22

Luo, Qilie, Joseph D. Andrade, and Karin D. Caldwell. "Thin-layer ion-exchange chromatography of proteins." Journal of Chromatography A 816, no. 1 (August 1998): 97–105. http://dx.doi.org/10.1016/s0021-9673(98)00286-6.

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23

Staahlberg, Jan. "Electrostatic retention model for ion-exchange chromatography." Analytical Chemistry 66, no. 4 (February 15, 1994): 440–49. http://dx.doi.org/10.1021/ac00076a005.

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24

Cai, Kang, Jennifer Anderson, Joshua D. Orchard, Christopher D. Afdahl, Matthew Dickson, and Yuling Li. "Virus removal robustness of ion exchange chromatography." Biologicals 58 (March 2019): 28–34. http://dx.doi.org/10.1016/j.biologicals.2019.01.004.

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25

Kim, Ung-Jin, and Shigenori Kuga. "Ion-exchange chromatography by dicarboxyl cellulose gel." Journal of Chromatography A 919, no. 1 (June 2001): 29–37. http://dx.doi.org/10.1016/s0021-9673(01)00800-7.

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26

Walton, Kevin M., and Ronald L. Schnaar. "Ganglioside glycosyltransferase assay using ion-exchange chromatography." Analytical Biochemistry 152, no. 1 (January 1986): 154–59. http://dx.doi.org/10.1016/0003-2697(86)90134-x.

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27

Brooks, Clayton A., and Steven M. Cramer. "Solute affinity in ion-exchange displacement chromatography." Chemical Engineering Science 51, no. 15 (August 1996): 3847–60. http://dx.doi.org/10.1016/0009-2509(95)00287-1.

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28

Gadam, Shishir D., Stuart R. Gallant, and Steven M. Cramer. "Transient profiles in ion-exchange displacement chromatography." AIChE Journal 41, no. 7 (July 1995): 1676–86. http://dx.doi.org/10.1002/aic.690410708.

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29

Harinarayan, C., J. Mueller, A. Ljunglöf, R. Fahrner, J. Van Alstine, and R. van Reis. "An exclusion mechanism in ion exchange chromatography." Biotechnology and Bioengineering 95, no. 5 (2006): 775–87. http://dx.doi.org/10.1002/bit.21080.

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30

Al-Omair, A. "Some ion-exchange resins for anion-chromatography." Talanta 34, no. 3 (March 1987): 361–64. http://dx.doi.org/10.1016/0039-9140(87)80047-4.

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31

Páll, Boglárka, Róbert Kormány, and Krisztián Horváth. "Az ionkromatográfia alkalmazhatóságának lehetőségei a gyógyszeranalitikában." Scientia et Securitas 3, no. 3 (April 6, 2023): 227–33. http://dx.doi.org/10.1556/112.2022.00110.

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Összefoglalás. Gyógyszermolekulák kémiai szintézissel történő előállítása során előfordulhat, hogy a szintézisút toxikus vegyületeket tartalmaz, vagy szintézis során képződik toxikus melléktermék. Ezeket az anyagokat alacsony koncentrációszinten kell kizárni a gyártott végtermékben, hogy az adott hatóanyag törzskönyvezése sikeres legyen. Így a genotoxikus (megváltoztatja a DNS által tárolt genetikai információt), rákkeltő szennyezők analitikai kontrollja folyamatos kihívás elé állítja az analitikusokat. Erre a vizsgálatra a legelterjedtebb módszer a nagyhatékonyságú folyadékkromatográfia. Ennek egyik speciális változata, a nagyhatékonyságú ionkromatográfia alkalmas a kis méretű ionos vagy ionizálható molekulák, pl. szervetlen anionok és kationok, szerves savak, aminok, valamint hidrolizálható vegyületek vizsgálatára. A kéziratban bemutatásra kerül a nagyhatékonyságú ionkromatográfiás technika, valamint annak gyógyszeranalitikai alkalmazása. Summary. In the production of drug molecules, the synthesis pathway may contain toxic compounds, or a toxic by-product may be formed during synthesis. These substances must be excluded at low concentration levels in the final manufactured product in order for the registration of the active substance to be successful. The drug analytics task to quantify these contaminations. This part of the pharmaceutical industry involves a wide spectrum of analytical techniques, which together complement each other to give a complete picture of the product being manufactured. Measurement techniques range from titration to large instrumentation (mass spectrometry, nuclear magnetic resonance spectrometry). Chromatography is one of the most widely used techniques. Lots of pollutant which must have quantified, have polar properties and its may present a risk for patients. The analytical control of genotoxic (altering the genetic information stored in DNA), carcinogenic contaminants is a constant challenge for analysts. Organic acids, amines, acid chlorides which are easily ionizable, hydrolysable are difficult to analyze at low concentration limits by the means of gas chromatography or high performance liquid chromatography. For the analysis of such contaminants, the high performance ion exchange chromatography method is a possible solution. In drug analytics, the ion chromatography techniques (ion exchange, ion exclusion, ion pair, ligand exchange) are not as widely used as the other liquid chromatography methods. In addition to inorganic anions and cations, ion chromatography is a suitable chromatographic method for the analysis of organic acids, amines, and hydrolysable compounds. In case of amines, this technique has better peak symmetry and theoretical plate height than gas chromatography. However, additional acidic API may cause the disappearance of these peaks. With this instrument, not only impurities can be tested, but also the counter ions of basic drug substances can be easily measured to verify the molecular composition of the active pharmaceutical ingredient. The manuscript describes the applications of ion exchange chromatography through some examples from pharmaceutical industry. In some cases, the methods have been validated according to international guidelines to demonstrate the applicability of high-performance ion exchange chromatography for the analysis of ionizable organic/inorganic compounds in pharmaceutical production.
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32

Little, R. R., and D. E. Goldstein. "Filter Paper/Affinity Chromatography vs. Venipuncture/HbA1 Ion-Exchange Chromatography." Diabetes Care 14, no. 8 (August 1, 1991): 767. http://dx.doi.org/10.2337/diacare.14.8.767a.

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33

Yu, L. Y., X. Zhang, J. Jin, S. Che, and L. Yu. " Simultaneous determination of chloride, bromide and iodide in foodstuffs by low pressure ion-exchange chromatography with visible light detection." Czech Journal of Food Sciences 29, No. 6 (November 28, 2011): 634–40. http://dx.doi.org/10.17221/216/2009-cjfs.

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An ion-exchange chromatography method with visible light detection was developed for the simultaneous determination of chloride, bromide, and iodide in foodstuffs. They were separated by means of low pressure ion-exchange chromatography using 4.0mM sodium carbonate solution as the eluent and a low pressure ion-exchange chromatography column as the separation column. The detection limits of chloride, bromide and iodide were 0.011 mg/l, 0.002 mg/l, and 0.023 mg/l, respectively. The relative standard deviations (RSDs) of the peak area were smaller than 2.9%. The recoveries were between 98.61% and 105.65%. Unlike the traditional methods, this validated method is inexpensive and stable.
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34

Bulleid, N. J., A. B. Graham, and J. A. Craft. "Microsomal epoxide hydrolase of rat liver. Purification and characterization of enzyme fractions with different chromatographic characteristics." Biochemical Journal 233, no. 2 (January 15, 1986): 607–11. http://dx.doi.org/10.1042/bj2330607.

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Microsomal epoxide hydrolase was purified from rat liver, and different fractions of the purified enzyme, which varied in their contents of phospholipid, were obtained by ion-exchange chromatography. One fraction (A), which did not bind to CM-cellulose, had a high phospholipid content, and a second fraction (B), which was eluted from CM-cellulose at high ionic strength, had a low phospholipid content. Removal of most of the phospholipid from fraction A altered its chromatographic behaviour. When the delipidated material was re-applied to CM-cellulose, most of the enzyme bound to the cation-exchanger. The specific activities of all the fractions described (with styrene epoxide [(1,2-epoxyethyl)benzene] as substrate) were altered by adding the non-ionic detergent Lubrol PX or phospholipid. Lubrol PX inhibited enzyme activity, and phospholipid reversed this inhibition. The various enzyme fractions isolated appeared to be different forms of the same protein, as judged by their minimum Mr values and immunochemical properties. These results indicate that different fractions of epoxide hydrolase isolated by ion-exchange chromatography probably are not different isoenzyme forms.
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35

Gerstner, Joseph A., Joseph Morris, Tony Hunt, Richard Hamilton, and Noubar B. Afeyan. "Rapid ion-exchange displacement chromatography of proteins on perfusive chromatographic supports." Journal of Chromatography A 695, no. 2 (March 1995): 195–204. http://dx.doi.org/10.1016/0021-9673(94)01225-4.

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36

Gerber, U., U. Jucknischke, S. Putzien, and H. L. Fuchsbauer. "A rapid and simple method for the purification of transglutaminase from Streptoverticillium mobaraense." Biochemical Journal 299, no. 3 (May 1, 1994): 825–29. http://dx.doi.org/10.1042/bj2990825.

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Transglutaminase from Streptoverticillium mobaraense was partially purified by ion-exchange chromatography on a weak acid material and hydrophobic chromatography. The separation with a strong acid ion-exchanger produces homogeneous transglutaminase, in a single step and with high yields, directly from the centrifuged and filtered culture fluid of the micro-organism. The procedure reproduced several times could be also carried out on a larger scale with the optimized parameters of the laboratory isolations. The purified enzyme demonstrated good storage stability.
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37

Hajós, P., and J. Inczédy. "Theory and applications of ion-exchange equilibria in ion chromatography." Reactive Polymers 17, no. 1 (April 1992): 120–21. http://dx.doi.org/10.1016/0923-1137(92)90592-p.

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38

Dianu, Aurelia Magdalena, and Relu Ion Dobrin. "Separation and quantification of 90Sr from ion-exchange resin radioactive waste: methods and techniques of analysis." Radiochimica Acta 108, no. 8 (August 27, 2020): 627–40. http://dx.doi.org/10.1515/ract-2019-3213.

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AbstractFour methods for 90Sr separation from spent ion-exchange resin samples were carried out, offering a useful methodology to achieve interferences free 90Sr fractions. The four methods consist in resin sample decomposition, pre-treatment and selective separation of 90Sr by using: (a) a single chromatographic extraction process, (b) double chromatographic extraction, (c) a single chromatographic extraction process followed in sequence by two precipitations, and (d) ion-exchange chromatography, followed by extraction chromatography and precipitation. Mineralization by microwave acid digestion and the four 90Sr separation methods thoroughly presented are available. Data processing methods (adjustable modified efficiency tracing – a new improved approach for the efficiency tracing LSC technique, non-linear regression and α-β discrimination) to obtain the activities values of α, β-γ, pure β emitters and the evaluation of chemical recovery yield of strontium were presented. A discussion about activity assessment in 90Sr purified fractions, providing a convincing argument to support the accuracy of the 90Sr separation methods, is also offered.
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39

Bruchet, Anthony, Vincent Dugas, Clarisse Mariet, Florence Goutelard, and Jérôme Randon. "Improved chromatographic performances of glycidyl methacrylate anion-exchange monolith for fast nano-ion exchange chromatography." Journal of Separation Science 34, no. 16-17 (May 27, 2011): 2079–87. http://dx.doi.org/10.1002/jssc.201100180.

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40

Studzińska, Sylwia, Szymon Bocian, Anna Kilanowska, and Bogusław Buszewski. "Dendrimer Anion-Exchange Stationary Phase for Separation of Oligonucleotides." Molecules 27, no. 5 (February 23, 2022): 1491. http://dx.doi.org/10.3390/molecules27051491.

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Oligonucleotides are used in many research areas. Thus, there is a need for their successful separation methods. Ion-exchange chromatography is the most popular separation technique, but it has limitations for these compounds. For this reason, new stationary phases are developed in order to increase separation selectivity. This study aimed to apply a series of dendrimer anion exchangers with various bonded layers to separate oligonucleotides by using different mobile phases to find conditions that allow sufficient separation. The number of anion-exchange layers, type of salt, and pH significantly impacted the oligonucleotide analysis. The developed chromatographic method was characterized by adequate selectivity for oligonucleotides differing in sequence length. It is essential to underline that the number of bonded layers appeared to have a significant influence, and the three layers appeared optimal. Based on our results, it may be concluded that the dendrimer stationary phases can be successfully used as an alternative to commonly applied packing materials in ion-exchange chromatography.
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41

Zumwalt, Robert W., Jean Desgres, Kenneth C. Kuo, James E. Pautz, and Charles W. Gehrke. "Amino Acid Analysis by Capillary Gas Chromatography." Journal of AOAC INTERNATIONAL 70, no. 2 (March 1, 1987): 253–62. http://dx.doi.org/10.1093/jaoac/70.2.253.

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Abstract Two developments have enabled major advancements in the use of capillary gas chromatography (GC), the result being its much more widespread use in investigations on a broad range of chemical and biological problems. The 2 technological developments were the introduction of fused silica capillary columns and the development of immobilized stationary phases for capillary GC columns. Because fused silica columns with immobilized stationary phases of varying polarities are offered by numerous vendors of chromatographic equipment, they have become widely used for many analytical tasks. We conducted a study to compare the effectiveness of commercially available fused silica capillary columns with the classical ion-exchange method in the separation and quantitation of amino acids. We selected the /V-trifluoroacetyl (TFA) n-butyl and the A'-heptafloorobutyryl (HFB) isobutyl ester derivatives for this study because of the extensive research and application of these derivatives during the past 20 years. The amino acid content of hydrolysates of 5 materials was measured: ribonuclease,β-lactoglobulin, lysozyme, soybean meal, and a commercial poultry feed. Single 6N HC1 hydrolysates of each material were prepared to minimize sample preparation differences, and 3 independent analyses of each hydrolysate were made by each of 3 techniques: the N-TFA n-butyl and N-HFB isobutyl ester methods using capillary gas chromatography and the ion-exchange chromatographic method using a Beckman 121 M amino acid analyzer. Our results clearly demonstrate that capillary GC analysis of amino acids using fused silica bonded-phase columns provides data with good precision and in general excellent agreement with ion-exchange analyses.
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42

Manuhara, Y. Sri. "ISOLASI DAN KARAKTERISASI ENZIM b-1,3-ENDOGLUKANASE DARI TANAMAN KUBIS (Brassica oleracea cv. Capitata L.)." Berkala Penelitian Hayati 15, no. 2 (June 30, 2010): 99–105. http://dx.doi.org/10.23869/bphjbr.15.2.20101.

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Isolation and characterization of β-1,3-endoglucanase from cabbage (Brassica oleracea var. capitata L.) have been done. It showed 40° C of optimum temperature, and optimum pH is 7. After the purification with hydrophobic interaction chromatography and ion exchange chromatography, it’s activity was increased. Based on SDS-PAGE analysis, β-1,3-endoglucanase have molecular weight around 48 kD. Antifungal activity of β-1,3-endoglukanase show that it has best inhibition zone on Fusarium solanii at extract from ion exchange chromatography.
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43

Zatirakha, A. V., A. S. Uzhel, A. D. Smolenkov, and O. A. Shpigun. "Anion-exchange sorbents for ion chromatography. Current trends." Analytics, no. 5 (2017): 34–44. http://dx.doi.org/10.22184/2227-572x.2017.36.5.34.44.

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44

Cook, Ken, and Jim Thayer. "Advantages of ion-exchange chromatography for oligonucleotide analysis." Bioanalysis 3, no. 10 (May 2011): 1109–20. http://dx.doi.org/10.4155/bio.11.66.

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45

Kumar, Vijesh, Samuel Leweke, William Heymann, Eric von Lieres, Fabrice Schlegel, Karin Westerberg, and Abraham M. Lenhoff. "Robust mechanistic modeling of protein ion-exchange chromatography." Journal of Chromatography A 1660 (December 2021): 462669. http://dx.doi.org/10.1016/j.chroma.2021.462669.

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46

Freed, Alexander S., and Steven M. Cramer. "Protein−Surface Interaction Maps for Ion-Exchange Chromatography." Langmuir 27, no. 7 (April 5, 2011): 3561–68. http://dx.doi.org/10.1021/la104641z.

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47

Steffenrud, S., P. Borgeat, and H. Salari. "Ion Exchange High Performance Liquid Chromatography of Leukotrienes." Journal of Liquid Chromatography 11, no. 4 (March 1988): 849–62. http://dx.doi.org/10.1080/01483918808068349.

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48

Rahman, A., and N. E. Hoffman. "Retention of Organic Cations in Ion Exchange Chromatography." Journal of Chromatographic Science 28, no. 4 (April 1, 1990): 157–61. http://dx.doi.org/10.1093/chromsci/28.4.157.

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49

Bos, Klaas D., Cornelis Verbeek, C. H. Peter Van Eeden, Pier Slump, and Mechteldis G. E. Wolters. "Improved determination of phytate by ion-exchange chromatography." Journal of Agricultural and Food Chemistry 39, no. 10 (October 1991): 1770–72. http://dx.doi.org/10.1021/jf00010a015.

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50

Levison, Peter R. "Large-scale ion-exchange column chromatography of proteins." Journal of Chromatography B 790, no. 1-2 (June 2003): 17–33. http://dx.doi.org/10.1016/s1570-0232(03)00087-4.

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