Relevant bibliographies by topics / Ion exchange gel chromatography

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Ion exchange gel chromatography'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Ion exchange gel chromatography"

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

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Russo, Salvatore F., and Angie Radcliffe. "Separations utilizing gel filtration and ion-exchange chromatography." Journal of Chemical Education 68, no. 2 (1991): 168. http://dx.doi.org/10.1021/ed068p168.

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SAEED, SHEIKH A. "Purification of human lactate dehydrogenase isoenzymes by preparative gel electrophoresis, gel chromatography and ion-exchange chromatography." Biochemical Society Transactions 16, no. 1 (1988): 18–19. http://dx.doi.org/10.1042/bst0160018.

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Deyl, Z. "Gel permeation and ion-exchange chromatography of proteins and peptides." Journal of Chromatography B: Biomedical Sciences and Applications 380 (January 1986): 472–73. http://dx.doi.org/10.1016/s0378-4347(00)83682-8.

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Zin El-Din, Mohamed, and Takayoshi Aoki. "High performance gel and ion-exchange chromatography of buffalo casein." International Dairy Journal 3, no. 2 (1993): 141–47. http://dx.doi.org/10.1016/0958-6946(93)90013-p.

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Ngai, Patrick H. K., and T. B. Ng. "Purification of glysojanin, an antifungal protein, from the black soybean Glycine soja." Biochemistry and Cell Biology 81, no. 6 (2003): 387–94. http://dx.doi.org/10.1139/o03-068.

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A monomeric protein, with a molecular mass of 25 kDa and an N-terminal sequence resembling a segment of chitin synthase, was isolated from the seeds of the black soybean Glycine soja. The protein, designated glysojanin, demonstrated potent antifungal activity against the fungi Fusarium oxysporum and Mycosphaerella arachidicola. It inhibited HIV-1 reverse transcriptase with an IC50 of 47 µmol/L, [methyl-3H]thymidine incorporation by mouse spleen cells with an IC50 of 175 µmol/L, and translation in the rabbit reticulocyte lysate with an IC50 of 20 µmol/L. Glysojanin was purified using a procedure that involved ion-exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion-exchange chromatography by fast protein liquid chromatography on Mono S, and gel filtration by fast protein liquid chromatography on Superdex 75.Key words: antifungal protein, seeds, soybean, purification.
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Sun, Jian, Hexiang Wang, and Tzi Bun Ng. "Trypsin Isoinhibitors with Antiproliferative Activity toward Leukemia Cells fromPhaseolus vulgariscv “White Cloud Bean”." Journal of Biomedicine and Biotechnology 2010 (2010): 1–8. http://dx.doi.org/10.1155/2010/219793.

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A purification protocol that comprised ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on SP-Sepharose, and gel filtration by FPLC on Superdex 75 was complied to isolate two trypsin inhibitors fromPhaseolus vulgariscv “White Cloud Bean”. Both trypsin inhibitors exhibited a molecular mass of 16 kDa and reduced the activity of trypsin with an value of about 0.6 M. Dithiothreitol attenuated the trypsin inhibitory activity, signifying that an intact disulfide bond is indispensable to the activity. [Methyl-] thymidine incorporation by leukemia L1210 cells was inhibited with an value of 28.8 M and 21.5 M, respectively. They were lacking in activity toward lymphoma MBL2 cells and inhibitory effect on HIV-1 reverse transcriptase and fungal growth when tested up to 100 M.
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Rüedi, P. "Non-aqueous ion exchange chromatography, an alternative to buffered silica gel." Journal of High Resolution Chromatography 8, no. 5 (1985): 256–58. http://dx.doi.org/10.1002/jhrc.1240080507.

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Osada, J., T. Gea, C. Sanz, I. Millan, and J. Botella. "Evaluation of dialysis treatment in uremic patients by gel filtration of serum." Clinical Chemistry 36, no. 11 (1990): 1906–10. http://dx.doi.org/10.1093/clinchem/36.11.1906.

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Abstract A group of substances of molecular masses between 300 and 1500 Da have been found to be toxic metabolites in patients with uremia. We determined the concentration in serum of these molecules in the following groups of patients: two hemodialyzed groups (one with cuprophane and the other with polyacrylonitrile dialyzers), one group treated with continuous ambulatory peritoneal dialysis, one group of nondialyzed azotemic patients, and one control group of healthy persons. Ultrafiltrates of the subjects' sera were fractionated on Sephadex G-15 followed by ion-exchange chromatography. Eluates were monitored by absorbance at 254 and 206 nm. Partially characterized peaks P1 and P2, obtained by gel filtration, correlated with the concentration of creatinine in serum; their concentrations were significantly (P less than 0.01) larger in hemodialyzed groups than in peritoneal dialyzed or in nondialyzed azotemic patients. After ion-exchange chromatography, two peaks (P'5 and P'6) correlated with serum creatinine and also were larger in hemodialyzed patients than in the other groups. Apparently, adequate discrimination is obtained by gel-filtration analysis and further analysis by ion-exchange chromatography does not provide additional information in most of the affected patients.
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Vancurová, I., J. Volc, M. Flieger, et al. "Isolation of pure anhydrotetracycline oxygenase from Streptomyces aureofaciens." Biochemical Journal 253, no. 1 (1988): 263–67. http://dx.doi.org/10.1042/bj2530263.

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Anhydrotetracycline oxygenase was purified to homogeneity from Streptomyces aureofaciens, a producer of tetracycline. The enzyme was purified 60-fold in a 40% yield by a two-step procedure using a combination of hydrophobic chromatography and ion-exchange h.p.l.c. Purified anhydrotetracycline oxygenase was homogeneous according to SDS/polyacrylamide-gel electrophoresis, isoelectric focusing, ion-exchange h.p.l.c. on a Mono Q HR 5/5 column and size-exclusion h.p.l.c. on a TSK G 3000 SW column. The enzyme consists of two subunits of Mr 57,500, as determined by SDS/polyacrylamide-gel electrophoresis.
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Dissertations / Theses on the topic "Ion exchange gel chromatography"

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MANOSSO, HELENA C. "Utilizacao dos trocadores inorganicos ZrP e TiP no tratamento de rejeitos industriais e radioativos." reponame:Repositório Institucional do IPEN, 2001. http://repositorio.ipen.br:8080/xmlui/handle/123456789/10919.

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Vergnolle, Chantal. "I: purification et caracterisation de proteines de transfert de phospholipides, a partir de feuilles d'epinard (spinacia oleracea l. ). Ii: synthese in vitro des proteines vegetales : methodologie." Paris 6, 1986. http://www.theses.fr/1986PA066254.

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Des proteines, capables de faciliter des mouvements intermembranaires de phospholipides, ont ete isolees a partir de feuilles d'epinard. Ces proteines, appelees proteines de transfert de phospholipides, ont ete purifiees par les techniques classiques de chromatographie (filtration sur gel, echangeurs d'ions) ou par les techniques plus resolutives et plus rapides de chromatographie liquide a haute performance (colonnes echangeuses d'ions ou en phase inverse). Nous avons verifie la purete des fractions par electrophorese en presence de sds
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Trevisoli, Edilaine Della Valentina Gonçalves. "Purificação de eliciadores de defesa vegetal em soja e feijoeiro a partir de nematoides fitopatogênicos." Universidade Estadual do Oeste do Paraná, 2016. http://tede.unioeste.br:8080/tede/handle/tede/1475.

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Made available in DSpace on 2017-07-10T17:40:55Z (GMT). No. of bitstreams: 1 Edilaine_D_V_GoncalvesTrevisoli.pdf: 2707364 bytes, checksum: 7b7a664f9727d5909c470f377ee155e8 (MD5) Previous issue date: 2016-02-25<br>Coordenação de Aperfeiçoamento de Pessoal de Nível Superior<br>The induction of resistance in plants to pathogens is an alternative method of disease control, wich involves activation of plant resistance mechanisms such as induction of phytoalexins. The elicitors molecules are able to induce and activate those responses, and therefore, techniques have sought to isolate and characterize fractions with elicitor character. The study aimed to purify, through ion exchange chromatography and gel filtration chromatography, eliciting molecules from pathogenic nematodes, and test them in phaseolin induction in beans hypocotyls beans and gliceolin in soybean cotyledons. The buffer solution Tris HCl 0.05 M (pH 6.8) was used as control and the acibenzolar-S-methyl (50 mg a.i. L-1) and Saccharomyces cerevisiae (20 mg mL-1) were used as induction standard treatments. Ion exchange chromatography (IEC) and gel filtration chromatography (GC) were performed to separate fractions with eliciting power from 500 female nematodes of Meloidogyne incognita and Meloidogyne javanica. For purification of elicitors from Meloidogyne javanica, through IEC, six glycidic fractions and six glycoproteins were obtained. These were purified on GC, obtaining sixty-three fractions. They have been classified according to their nature, as twenty-six glycidic and thirty-seven glycoprotein with molecular weights ranging from 29.19 to 2989.25 kDa. Regarding the elicitors purification of Meloidogyne incognita through IEC, nine glycidic and five glycoprotein fractions were obtained. From these fractions, a total of fifty-eight fractions was obtained through GC, twenty-five glycidic and thirty-three glycoprotein with molecular weights ranging from 37.42 to 200.32 kDa. From the fractions purified from Meloidogyne javanica eight had inducing potential of phaseolin. For gliceolin fifteen fractions showed inducing effect. Regarding the fractions purified from Meloidogyne incognita, no fraction has inductive potential of phaseolin superior to the standard treatment. However, twenty-two fractions suppressed phytoalexin inducing activity. For gliceolin ten fractions induced the same, whereas, twenty-three fractions suppressed the induction of gliceolin. Chromatography was efficient in the purification of elicitors compounds. Compounds with suppressing characteristics of gliceolin and phaseolin were checked in bioassays. For those fractions obtained through IEC, and then submitted to GC that did not induce phytoalexin, it is suggested that molecules need to act together to have elicitor effect and thus induce defense response in the plant<br>A indução de resistência em plantas contra patógenos é um método de controle alternativo de doenças, e que envolve a ativação dos mecanismos de resistência da planta, como a indução de fitoalexinas. As moléculas eliciadoras possuem a capacidade de induzir e ativar tais repostas, e assim sendo, técnicas têm buscado isolar e caracterizar frações com caráter eliciador. O trabalho teve por objetivo purificar, por cromatografia de troca iônica cromatografia de filtração em gel, moléculas eliciadoras a partir de nematoides fitopatogênicos, e testá-las na indução de faseolina em hipocótilos de feijoeiro e gliceolina em cotilédones de soja. O tampão Tris HCl 0,05 M (pH 6,8) foi utilizado como tratamento controle e o acibenzolar-S-metil (50 mg i.a. L-1) e o Saccharomyces cerevisiae (20 mg mL-1) foram utilizados como tratamento padrão de indução. Cromatografia de troca iônica (CTI) e cromatografia de filtração em gel (CFG) foram realizadas para separar frações com poder eliciador a partir de quinhentas fêmeas de nematoides de Meloidogyne incognita e Meloidogyne javanica. Para a purificação de eliciadores a patir de Meloidogyne javanica, por CTI, foram obtidos seis frações glicídicas e seis glicoproteicas. Estas, por sua vez, foram purificadas em CFG, sendo obtidos no total sessenta e três frações. As mesmas foram classificadas de acordo com sua natureza, sendo vinte e seis glicídicas e trinta e sete glicoproteicas, com massas moleculares variando de 29,19 a 2.989,25 kDa. Em relação a purificação de eliciadores de Meloidogyne incognita por CTI, foram obtidos nove frações glicídicas e cinco glicoproteicas. A partir destas, foram obtidos por CFG um total de cinquenta e oito frações, sendo vinte e cinco glicídicas e trinta e três glicoproteicas, com massas moleculares variando de 37,42 a 200,32 kDa. Das frações purificadas a partir de Meloidogyne javanica oito apresentaram potencial indutor de faseolina. Para gliceolina quinze frações mostraram efeito indutor. Em relação as frações purificadas a partir de Meloidogyne incognita, nenhuma fração apresentou potencial indutor de faseolina superior ao tratamento padrão. Entretanto, vinte e duas frações suprimiram a atividade de indução de fitoalexina. Para gliceolina dez frações induziram a mesma, enquanto que, vinte e três frações suprimiram a indução da gliceolina. A cromatografia foi eficiente na purificação de compostos eliciadores. Compostos com características supressoras de gliceolina e faseolina foram verificadas nos bioensaios. Para aquelas frações obtidas por CTI e posteriormente submetidas a CFG que não induziram fitoalexina, sugere-se que as moléculas necessitam atuar juntas para haver efeito eliciador e assim induzir a resposta de defesa no vegetal
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Kruger, Sarah Jane, and n/a. "Characterisation of Proteins from Grevillea robusta and NMR Studies of the Serine Protease Inhibitor." Griffith University. School of Science, 2004. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20040618.150708.

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Proteins that recognise the sugar surface structures on cells have an enormous potential to be used as tools in the characterisation of these structures. A group of proteins, called lectins, have been identified that can bind to carbohydrate complexes on the receptors of cells. The crude extract from Grevillea robusta seeds was found to contain lectin-like proteins that were different from most other lectins, as they would specifically target the receptors of white blood cells and not those found on red blood cells. Therefore, the lectin isolated from G.robusta could be used as a tool to identify the specific surface structures on white blood cells. The lectin was isolated using affinity chromatography where a complex (oligosaccharide) matrix was used. Agglutination, binding and sugar inhibition assays confirmed the isolated protein was a lectin. The lectin was found in low amounts (up to 5% of the total protein content) within the seeds of G.robusta. As a result of this low yield, the identification of the lectin by PAGE was difficult because the levels of protein were beyond the detection limit of the commercial staining reagents. The lectin was called the GR2 protein and was characterised as a monocot mannose binding lectin based on its sugar specificity for only mannose. A serine protease inhibitor was isolated from the seeds of G.robusta using two different chromatography methods, reverse phase HPLC (GR1.HPLC) and gel filtration chromatography (GR1.GF). Ion exchange chromatography was used to initially separate the proteins in the crude extract and the fraction containing the GR1 protein was further purified using reverse phase HPLC (GR1.HPLC). N-terminal sequencing results of the GR1.HPLC protein, showed evidence of proteolytic cleavage during the extraction process, which lead to the second purification method being established. Protease inhibitors were added to the buffers prior to being purified by gel filtration chromatography, which resulted in the GR1 protein being isolated from the crude extract without the presence of the contaminating protein. Mass spectroscopy identified the molecular weight of the GR1 protein to be 6669Da and the full amino acid sequence was derived by cDNA techniques. Sequence alignment studies of the GR1 protein showed significant similarities with the Bowman-Birk inhibitor. The positioning of the cysteine residues were conserved throughout the Bowman-Birk superfamily, however these residues were not conserved within the GR1 protein. Competitive inhibition assays on the GR1 protein revealed the protein could inhibit both trypsin and chymotrypsin at similar levels to that seen for the Bowman-Birk inhibitor. Therefore, the GR1 protein was characterised as a member of the Bowman-Birk superfamily of serine protease inhibitors. The three-dimensional structure of the GR1 protein was determined using two-dimensional NMR spectroscopy. Computer programs such as XEASY, DYANA and SYBYL® were used to tabulate the information taken from the 2D experiments, generate structures and minimise these structures respectively. The solution structure of the GR1 protein was found to contain a region of antiparallel β-sheet structure that corresponded to the trypsin binding site and the remainder of the protein consisted of loops and turns that were held together by disulfide bridges (the chymotrypsin-binding region). Structural similarities between the GR1 protein and the Bowman-Birk inhibitor existed only in the trypsin-binding site of the Bowman-Birk inhibitor. The GR1 protein is the first member of the Proteaceae family to be characterised as a Bowman-Birk inhibitor. This thesis outlines the isolation and biochemical characterisation of the two proteins found within Grevillea robusta and also describes the steps involved and results obtained in determining the three-dimensional structure of the GR1 protein.
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Baba, Hamed Mohamed Bey. "Purification et caractérisation de protéases alcalines des larves de Galleria Mellonella." Rouen, 1986. http://www.theses.fr/1986ROUES053.

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Deux protéases alcalines P1 et P2 ont été isolées à partir d'homogénats de larves de Galleria mellonella. Les 2 enzymes ont été séparées par chromatographie sur échangeurs d'ions et purifiées ultérieurement par filtration sur gel. Les 2 protéases se distinguent par leur pH optimum d'action, leur poids moléculaire et leur sensibilité vis-a-vis de différents inhibiteurs de protéases. La répartition anatomique de l'activité protéolytique montre la présence de 2 protéases alcalines similaires à P1 et P2 dans le tube digestif, et d'une protéase similaire à P1 dans le tissu adipeux
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Polite, Lee Nicholas. "Studies in ion exchange chromatography." Diss., Virginia Polytechnic Institute and State University, 1988. http://hdl.handle.net/10919/54338.

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This dissertation investigates three major problems in IC, ranging from the practical to the theoretical. The first is of interest to the field of quantitative analysis. Since ion chromatography is primarily a quantitative technique, the linear range of the detector is of particular interest. The linear range was determined to be nearly five orders of magnitude for several common ions. The probes used were fluoride, chloride, sulfate, sodium, and potassium with concentrations ranging from 10 ppb to 1000 ppm. This portion of the dissertation describes the first attempt made to elucidate the linear detection range in ion chromatography using micro-membrane suppression. The Iinearity experiments demonstrate the versatility of ion chromatography with respect to quantifiable concentrations. However, a major problem is encountered when attempting to determine a trace ion concentration in the presence of a high concentration of a similarly charged ion (matrix ion). The second part of this dissertation offers a solution to this problem. In ion chromatography, the large excess of a matrix ion affects not only the ions expected in that region of the chromatogram, but also destroys the chromatographic exchange process. One objective of this study was to develop a rapid quantitative method to determine 5 ppm chloride in the presence of 100,000 ppm sulfate. A standard anion exchange column will completely lose resolution between chloride and sulfate at a sulfate concentration of approximately 2500 ppm. The apparatus designed and built by the author uses two analytical ion—exchange columns coupled in series by a high pressure switching valve. ln order to complete the system, the author designed and built y a high pressure conductivity detector cell to monitor the conductivity of the effluent from the first column. The system works by overloading the first column and then allowing the effluent to pass onto the second column. When the trace chloride in on the second column, the first column is switched out of line. This process allows the trace chloride to be separated from the residual sulfate. The column switching study brought to light several theoretical questions about the inner workings of the packing materials used in ion chromatography. These questions include the effects that flow rate and temperature have on capacity and efficiency in ion chromatography separations. Using chloride and sulfate as probes, the chromatographic efficiency was shown to decrease from 30° to 60° C. Even more surprising was the result that sulfate retention increased with increasing temperature while chloride retention decreased under the same conditions. Detailed studies as well as possible explanations are included in the third part of this dissertation.<br>Ph. D.
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Maketon, Supachai. "Methods Development for Ion Chromatography." Thesis, North Texas State University, 1986. https://digital.library.unt.edu/ark:/67531/metadc330927/.

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Ion chromatography (IC) as developed by Small et. al. in 1975 has become an efficient and reliable analytical technique for simultaneous analysis of multiple ions in solution. The principle requirement prior to use the IC for an analysis is sample preparation; these include sample decomposition, solvent extraction, and trapping in case the target element is in the gas phase, etc. Solvent extractions for fluoride, chloride, sodium, ammonium, and potassium ions which are soluble in soils are described. Sample decompositions include silicate rocks using hydrofluoric acid for the determination of phosphorus; organic pesticides using lithium fusion technique for the determination of halide and cyanide ions are also described. After these sample preparation techniques, the aqueous solutions obtained were analyzed on the ion chromatograph for the analyses of the anions and cations mentioned above. Recovery and reproducibility of each technique is in general quite good and the comparison between the results obtained from the IC method and other instrumentation are given.
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Forrer, Nicola. "Antibody purification with ion-exchange chromatography." Zürich : ETH, 2008. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=17784.

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Cao, Liming. "Protein Separation with Ion-exchange Membrane Chromatography." Link to electronic thesis, 2005. http://www.wpi.edu/Pubs/ETD/Available/etd-050405-174109/.

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Pearson, C. H. G. "New ion exchange resins for ion chromatography applied to anions." Thesis, University of Kent, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.372771.

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Books on the topic "Ion exchange gel chromatography"

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Fritz, James S. Ion chromatography. 4th ed. Wiley-VCH, 2009.

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Ion chromatography. 2nd ed. VCH, 1995.

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1924-, Fritz James S., and Fritz James S. 1924-, eds. Ion chromatography. 2nd ed. A. Hüthig, 1987.

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T, Gjerde Douglas, and Gjerde Douglas T, eds. Ion chromatography. 3rd ed. Wiley-VCH, 2000.

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Ion chromatography. Plenum Press, 1989.

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E, Smith Robert. Ion chromatography applications. CRC Press, 1988.

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Handbook of ion chromatography. 3rd ed. Wiley-VCH, 2004.

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1945-, Nakanishi Kazuhiro, and Matsuno Ryūichi 1939-, eds. Ion-exchange chromatography of proteins. M. Dekker, 1988.

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E, Jackson Peter, ed. Ion chromatography: Principles and applications. Elsevier, 1990.

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David, Rocklin Roy, ed. Ion exchange in analytical chemistry. CRC Press, 1990.

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Book chapters on the topic "Ion exchange gel chromatography"

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Watson, J. S. "Improvements in Macroreticular Particles for Ion-Exchange and Gel-Permeation Chromatography." In Recent Developments in Ion Exchange. Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0777-5_26.

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Mohammad, Ali, Abdul Moheman, and Gaber E. El-Desoky. "Cation-Exchanged Silica Gel–Based Thin-Layer Chromatography of Organic and Inorganic Compounds." In Ion Exchange Technology II. Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4026-6_16.

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Small, Hamish. "Ion Exchange in Ion Chromatography." In Ion Chromatography. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4899-2542-8_4.

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Sheehan, David. "Ion-Exchange Chromatography." In Springer Protocols Handbooks. Humana Press, 2008. http://dx.doi.org/10.1007/978-1-60327-375-6_40.

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Schönbächler, Maria. "Ion Exchange Chromatography." In Encyclopedia of Earth Sciences Series. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-39312-4_113.

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Schönbächler, Maria. "Ion Exchange Chromatography." In Encyclopedia of Earth Sciences Series. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-39193-9_113-1.

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Sheehan, David, and Richard Fitzgerald. "Ion-Exchange Chromatography." In Springer Protocols Handbooks. Humana Press, 1998. http://dx.doi.org/10.1007/978-1-59259-642-3_35.

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Morss, Lester R. "Ion Exchange Chromatography." In Inorganic Reactions and Methods. John Wiley & Sons, Inc., 2007. http://dx.doi.org/10.1002/9780470145296.ch10.

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Dörr, Mark. "Ion-Exchange Chromatography." In Encyclopedia of Astrobiology. Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_805.

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Karlsson, Evert, and Irwin Hirsh. "Ion Exchange Chromatography." In Methods of Biochemical Analysis. John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9780470939932.ch4.

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Conference papers on the topic "Ion exchange gel chromatography"

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TSUNEIZUMI, I., T. MEGURO, and K. YAMADA. "SUDAY ON A SUBSTANCE FUNCTIONALLY LIKE PROTEIN C IN PLASMA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644303.

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The present report first deals with the isolation and characterization of a substance found to demonstrate protein C like activity(PCLA). When it was activated by thrombin, the PCLA substance prolonged the activated partial thromboplastin time(aPTT). The activated PCLA substance also hydrolyzed synthetic substrates such as S�2238, S�2366 and S�2266,while the PCLA substance was not cross reacted with anti-protein C serum(Behring Manheim). The PCLA substance was adsorbed by both aluminium hydroxide gel and barium sulfate. The level of Km, optimum pH and optimum I.S. in the amido-lytic reaction with synthetic substrate is shown in the table.In the chromatography of Sepharose CL-6B gel, the PCLA substance was eluted in the fraction of higher molecular weight, while protein C was eluted with a lower fraction.This prompts an estimate that the molecular weight of the PCLA substance is approximately 200,000. Through DEAE-Sepharose CL-6B gel ion exchange chromatography, the PCLA substance was eluted by a lower ionic strength than was protein C.The levels of a PCLA substance were low in the patients with a vitamin K deficiency and in newborn infants. It is expected that our findings regarding the PCLA substance will be as clinically significant as that which we know about protein C at present.
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Jørgensen, M. "HEPARIN INDEPENDENT PURIFICATION OF ANTITHROMBIN III (AT III) BY IMMUNO-AFFINITY CHROMATOGRAPHY RESULTING IN A FUNCTIONALLY INTACT MOLECULE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643682.

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Previous methods for purification of AT III are based on its heparin-binding capacity. However, in congenital AT III deficiency abnormal inhibitor molecules with impaired binding of heparin and/or thrombin has been reported. The aim of the present study was to develop a purification method based on immuno-affinity chromatography, and thus independent of the heparin binding capacity.Rabbits were immunized with human AT III purified by a three-step procedure involving dextran sulphate precipitation, affinity chromatography on heparin-Sepharose and ion-exchange chromatography on DEAE-Sephadex A-50. Rabbit immunoglobulins against human AT III were isolated by affinity chromatography using purified human AT III coupled to CNBr-activated Sepharose 4B. Trace amounts of immunoglobulin against human albumin, IgG and IgM were removed by solid phase immunoadsorption. The highly purified immunoglobulins against human AT III were coupled to CNBr-activated Sepharose 4B. This anti-AT III-Sepharose was used for single-step purification of AT III from plasma. Elution was performed by Na-citrate buffer at pH 3.0 and the eluted fractions immediately neutralized. The recovery was more than 60%.The purified AT III appeared as a single protein band in SDS-poly-acrylamide gel electrophoresis with or without reduction. Affinity purified AT III and AT III purified by the three-step procedure were indistinguishable when analyzed by crossed immunoelectrophoresis in the absence and the presence of heparin isoelectrical focusing in polyacrylamid gel at a pH 4-6.5 gradient, and SDS-polyacrylamide gel electrophoresis. AT III antigen concentration was determined by electroimmunoassay and the reactive site concentration determined by titration with purified human thrombin using Phe-Pip-Arg-Nan (S-2238) as substrate. The ratio (active site conc.)/(antigen conc.) was identical in the two AT III preparations. It is concluded that this single-step immuno-affinity chromatography gives a high recovery from plasma of a highly purified functionally intact AT III molecule. The purification method is independent of the heparin binding capacity of AT III. This is of particular importance for the purification and characterization of abnormal AT III molecules with impaired heparin-binding site.
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3

Clezardin, P., and J. L. McGregor. "STRUCTURAL AND FUNCTIONAL COMPARISON OF THROMBOSPONDIN FROM PLATELETS, ENDOTHELIAL CELLS AND FIBROBLASTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643819.

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Thrombospondin (TBSP) is a 450 kDa glycoprotein secreted by a wide range of cells including platelets, endothelial cells and fibroblasts. Using non-denaturating conditions, we recently reported that platelet TBSP was structurally different from endothelial and fibroblast TBSP (P. Clezardin et al., Eur. J. Biochem., 1986, 159, 569-579). The aim of this study was to compare the structure of TBSP purified from platelets, endothelial cells and fibroblasts using denaturating conditions. Moreover, the interaction of fibrinogen with these three forms of TBSP was also investigated. TBSPs were first purified by heparin-Sepharose and immunoaffinity chromatography followed by Mono O anion-exchange chromatography on a FPLC system. Thermolysin digests of purified TBSPs were analysed by SDS-polyacrylamide gel electrophoresis under reducing conditions and the subsequent electrophoresed proteolytic fragments identified by Coomassie and silver staining. The interaction of undigested and digested TBSPs with solid-phase adsorbed fibrinogen was investigated by enzyme-linked immunosorbent assay using an anti-TBSP monoclonal antibody (P10). when using Coomassie staining, a 70 kDa proteolytic fragment of thermolysin-treated platelet TBSP was absent from the endothelial and fibroblast TBSP digests. Moreover, a 18 kDa fragment from thermolysin-treated endothelial and fibroblast TBSP was undetectable in the platelet TBSP digest when using silver staining on SDS-polyacrylamide gels. The binding of undigested TBSPs to solid-phase adsorbed fibrinogen was different from that obtained with digested TBSPs. These results indicate that the observed structural differences might induce functional differences between platelet and the two other forms of TBSP.
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Masci, P. P., A. N. Whitaker, J. J. Morrison, and E. A. Bennett. "PURIFICATION AND CHARACTERIZATION OF THE PROCOAGULANT OF THE VENOM OF TROPIDECHIS CARINATUS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644322.

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Tropidechis carinatus is a venomous elapid snake distributed throughout Eastern Queensland. It has been considered as a tropical relative of Notechis scutatus and, similarly, the crude venom contains an indirect prothrombin activator, which will clot plasma provided that Factor V is present. Myotoxins and neurotoxins are also present. Envenomated patients regularly develop disseminated intravascular coagulation. The crude whole venom of T.carinatus was shown to have five major components by gel filtration, SDS PAGE and HPLC, and even more components by isoelectric focusing. The procoagulant eluted with a molecular weight of 55,000, being found in peak II on gel filtration on Sephadex-G150. The procoagulant was purified using a combination of Sephadex-G150 chromatography and ion-exchange on DEAE Sephadex-A50 and shown to migrate as a single band of molecular weight 55.000 by SDS PAGE. On reduction by β -mercaptoethanol this component was resolvec into u heavy chain of molecular weight 30.000 and a light chain of 25,000. The procoagulant was shown to bind to con A-Sepharose 4B and Blue Sepharose 4B. Coagulation studies using this purified procoagulant confirmed a factor Xa-like activity activating prothrombin in the presence of factor V. The purified fraction is unstable in buffer solutions at 4°C, probably because of trypsin - like autodigestion. Ouchterlony studies of the procoagulants of T.carinatus and N.scutatus show both lines of homogeneity and spurring, indicating similarities but also significant differences between the two proteins. The purified procoagulant was lethal to adult rats, an IV injection of 10 μg killing in 1 - 2 minutes. Death was prevented by prior heparinization, suggesting that the procoagulant is toxic in the absence of neurotoxin and other components.
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Wilhelm, S., and A. Henschen. "ON THE IDENTIFICATION OF POLYMORPHIC SITES IN HUMAN FIBRINOGEN PEPTIDE CHAINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643327.

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Human fibrinogen has repeatedly been shown to occur in a great number of different molecular forms. Some types of heterogeneity are evident already from variations in solubility properties and in ion-exchange-chromatographic as well as gel-electrophoretic behaviour of the total molecule and of its peptide chain components. The reason for these variations are partly known.Thus, degradation of the C-terminal parts and phosphorylation of two serine residues gives rise to heterogeneity in the Aα-chain. Differences in the sialylation of the carbohydrate side chain causes heterogeneity both in the Bβ- and the γ-chain. Differences in chain length at the C-terminus of the γ-chain are responsible for additional variation. All these variants are expected to exist in each human being. An other category of human fibrinogen variants may be due to genetic polymorphism within the population, i.e. the presence of inherited, common, normal variants. Seven sites of microheterogeneity have so far been tentatively identified, mainly by disagreements between protein and DNA sequence analyses. Three of the sites are located in the Aα-chain (positions 47, 296 and 312), three in the Bβ-chain (positions 162, 296 and 44-8) and one in the γ-chain (position 88). The aim of the present study was to identify these sites on the proteinchemical level in pooled plasma as well as in plasma from single individuals, especially various members of the same family. For this purpose suitable fibrinogen fragments containing the tentatively microheterogeneous sites were isolated after cleavage of fibrinogen with cyanogen bromide, trypsin and/or chymotrypsin by repeated fractionations by means of conventional and reversed-phase high-performance liquid chromatography and counter-current distribution. The components were characterized by N-terminal sequence and amino acid composition. Polymorphism in human fibrinogen has previously only once been identified by restriction fragment length analysis in a non-transcribed region of the Aα-chain locus but never in the transcribed regions, i.e. the peptide chains.The present investigation will allow the estimation of the number of peptide chain haplotypes and their possible correlation to other genetic variants of fibrinogen.
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Kemball-Cook, G., S. J. A. Edwards, K. Sewerin, L.-O. Andersson, and T. W. Barrowcliffe. "THE PHOSPHOLIPID-BINDING SITE OF FACTOR VIII IS LOCATED ON THE 80 kD LIGHT CHAIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643615.

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The binding of Factoi. VIII (F.VIII) peptides to phospholipid (PL) vesicles has been studied by two different methods involving the use of fractionated anti-F.VIII:C I-Fab123’pre viously reported, i-Fab123’ was fractionated by immunoadsorptionwith F.VIII-PL complexes into two pools:one binding only to PL-binding sites on F.VIIIsAg (PL-site antibody), the other directed against other antigenic sites (non-PL-site antibody).The first technique used was a modification of the method of Weinstein et al. (Proc.Natl.Acad.Sci.USA, 78, 5137-5141, 1981), and involved incubation of the two anti-F.VIII pool swith F.VIII-containing samples, followed by electrophoretic separation of the complexes on the basis of size in non-denaturing SDS gels: this technique allows qualitative analysis of antibody reactive peptides in highly impure samples. Non-PL-site pool reacted with a range of peptides with MrMapparent Mr 90 kD up to 280 kD, a similar pattern to that of ’heavy chain’(HC) peptides of F.VIII seen on SDS-PAGE under reducing conditions; the PL-site antibody, however, reacted only with peptides at apparent Mrs of 80 kD and sometimes150 kD, but not with bands of higher Mr a pattern more consistent with binding to light chain (LC) peptides. Thesame patterns with the two labels were seen in both plasma and F.VIII concentrateThe second approach employed the two labels described above in direct immunoradiometric assays (IFMA’s) on purified human F.VIII peptides prepared by immunoaffinity chromatography and ion exchange on Mono Q gel. Both PL-site and non-PL-site labels measured similar amounts of F.VIII m a sample containing both HC and LC peptides; however, on assaying a sample containing purified HC peptides alone, PL-site antibody measured only 2% of F.VIII:Ag found by non-PL-site label, indicating that PL-binding sites present in samples containing both HC and LC are absent in HC alone.Results from both these immunological methods indicate that the 80 kD LC peptide of F.VIII carries the PL-binding site.
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7

Niiya, K., P. Kostel, T. S. Zimmerman, and Z. M. Ruggeri. "CHARACTERIZATION OF A 40 kDa FRAGMENT OF VON WILLEBRAND FACTOR THAT CONTAINS THE GLYCOPROTEIN IIb/IIIa-BINDING DOMAIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642874.

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We have isolated a 40 kDa fragment of von Willebrand factor (vWF) that contains the glycoprotein (GP) Ilb/IIIa-binding domain. The Staphylococcus aureus V8 protease-generated fragment II was digested with trypsin (1:50 enzyme:substrate ratio on a weight-to-weight basis). After addition of a 100fold molar excess of (p-amidinophenyl)methanesulfonyl fluoride in order to inhibit any residual trypsin activity, the whole digest was subjected to ion-exchange and size-exclusion high pressure liquid chromatography. Two major fragments were separated. Analysis by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS) demonstrated that one of the two purified polypeptides had an apparent molecular weight of 40 kDa under both reducing and nonreducing conditions, suggesting that it was a single chain polypeptide. The other fragment had an apparent molecular weight of 22 kDa after reduction and 44 kDa unreduced, suggesting that it was a homodimer. Amino terminal sequence analysis of both fragments was performed by classical Edman degradation following electroelution from reduced SDS-polyacrylamide gels. The amino terminus of the 40 kDa fragment corresponded to residue Glu (1366) (as did the fragment II from which it was derived), while the amino terminus of the 22 kDa fragment corresponded to residue Val (1927) of the constituent 2050 residue subunit. The effect of both fragments on vWF binding to the platelet membrane GP IIb/IIIa complex was evaluated by measuring the residual binding of 125I-labeled vWF to thrombin-stimulated platelets in the presence of varying amounts of the unreduced fragments. The 40 kDa polypeptide inhibited 64 percent of vWF binding when tested at a concentration of 20 μK, whereas the 22kDa dimer was without effect. This study establishes that the GP IIb/IIIa-binding domain of vWF resides in a discrete, single-chain 40 kDa fragment derived from the 220 kDa, homodimeric fragment II generated by V8 protease. Moreover, we found evidence for the existence of inter-chain disulfide bonds within 22 kDa from the carboxyl terminus of the constituent subunit.
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8

Kempfer, A. C., N. Maugeri, C. Farías, E. Bermejo, M. Gimeno, and M. Lazzari. "PURIFICATION AND PARTIAL CHARACTERIZATION OF A BIOACTIVE SUBSTANCE FROM RAT'S VESSEL WALL INDEPENDENT OF PROSTACYCLIN PRODUCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643362.

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Our previous observations provided evidence that a bioactive substance (BAS) with inhibitory effect on platelet aggregation and with inotropic activity on smooth muscle preparations is present in aortic wall of rats treated previously with indomethacin. The ability to inhibit platelet aggregation was used for monitoring its purification and partial characterization. The original sample was extracted by rinsing aortic rings (1.5 mg dried rings) in buffer Krebs (300 μl) for 40 minutes at room temperature. The substance was purified by gel filtration (Bio-gel P-30, Sephadex G-100, Sephadex G-75) and ion exchange chromagra-phy (DEAE cellulose). In the last method, salt gradient elution was performed. Further purification by Sephadex G-50 resulted in removal of 90% of the contaminating substances without a loss of inhibitory activity. The main peak of both chromatographic procedures was analyzed on SDS-PAGE and PAGE with denaturing solvents. The substance was evident by Coomassie Brilliant Blue and periodic acid Schiff staining.In order to determine if the BAS was susceptible to proteolysis, an aliquot of the original sample (29 ug total protein) was incubated with trypsin (final concentration 0.3 μg/ml) and with chymotrypsin (final concentration 3 μg/ml). The BAS activity was not detected. An aliquot of the same original sample was incubated with neuraminidase (final concentration 1.2 units). The BAS activity was detected.The substance appeared to be stable for at least 18 hours at room temperature and 2 hours at 37°C, In addition it was stable over a pH range between 6.8 to 8.6, showing an anionic behaviour.The protein concentration of this substance determined by the method of Lowry was 1 μg/mlPartial characterization supports the conclusion that the substance present in aortic wall of rats is a homogeneous protein, which has a molecular size estimated at 55-65 kDa.
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9

MAXIMO, E., J. A. BENDASSOLLI, and P. C. O. TRIVELIN. "ENRICHMENT OF 15N BY COUPLING THREE SYSTEMS OF ION-EXCHANGE CHROMATOGRAPHY COLUMNS." In Proceedings of the 3rd International Conference on Isotopes. WORLD SCIENTIFIC, 2000. http://dx.doi.org/10.1142/9789812793867_0032.

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10

Malvestio, A. C., M. Barboza, J. A. C. Leite, and M. Zaiat. "Volatile fatty acids separation by ion exchange chromatography in fixed bed column." In Proceedings of the III International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld2009). WORLD SCIENTIFIC, 2010. http://dx.doi.org/10.1142/9789814322119_0050.

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