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Journal articles on the topic 'Gel permeation chromatography'

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Published: 4 June 2021
Last updated: 30 July 2024

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1

Someya, Taiyo, and Shunsuke Kita. "Gel Permeation Chromatography." Drug Delivery System 38, no. 3 (July 25, 2023): 250–53. http://dx.doi.org/10.2745/dds.38.250.

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2

Lesec, James. "Preparative Gel Permeation Chromatography." Journal of Liquid Chromatography 8, no. 5 (April 1985): 875–923. http://dx.doi.org/10.1080/01483918508067121.

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3

Qingguo, Wang, Cai Lixing, David Thompson, You Xinkui, Chen Zhihang, Chen Junbo, and Qiu Qiaomei. "DIFFERENTIAL GEL PERMEATION CHROMATOGRAPHY." Journal of Liquid Chromatography & Related Technologies 24, no. 3 (January 2001): 317–25. http://dx.doi.org/10.1081/jlc-100001336.

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4

Ogawa, Toshio. "Gel Permeation Chromatography of Polyoxymethylene." Journal of Liquid Chromatography 13, no. 1 (January 1990): 51–61. http://dx.doi.org/10.1080/01483919008051786.

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5

Moore, J. C. "Gel permeation chromatography: Its inception." Journal of Polymer Science Part C: Polymer Symposia 21, no. 1 (March 8, 2007): 1–3. http://dx.doi.org/10.1002/polc.5070210103.

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6

Tröltzsch, Christof. "Atypic Gel Permeation Chromatography of Alcohols." Journal of Liquid Chromatography 9, no. 6 (May 1986): 1367–80. http://dx.doi.org/10.1080/01483918608075509.

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7

Ye, Meiling, Youkang Ding, Jianwen Mao, and Lianghe Shi. "High-performance vacancy gel permeation chromatography." Journal of Chromatography A 518 (January 1990): 238–41. http://dx.doi.org/10.1016/s0021-9673(01)93181-4.

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8

Anger, H., and G. Berth. "Gel permeation chromatography of sunflower pectin." Carbohydrate Polymers 5, no. 4 (January 1985): 241–50. http://dx.doi.org/10.1016/0144-8617(85)90033-5.

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9

Meyerhoff, G. "The efficiency of gel permeation chromatography." Journal of Polymer Science Part C: Polymer Symposia 21, no. 1 (March 8, 2007): 31–41. http://dx.doi.org/10.1002/polc.5070210107.

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10

Bata, G. L., J. E. Hazell, and L. A. Prince. "Polymer characterization by gel permeation chromatography." Journal of Polymer Science Part C: Polymer Symposia 30, no. 1 (March 7, 2007): 157–62. http://dx.doi.org/10.1002/polc.5070300119.

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11

Montague, P. G., and F. W. Peaker. "Large scale preparative gel permeation chromatography." Journal of Polymer Science: Polymer Symposia 43, no. 1 (March 8, 2007): 277–89. http://dx.doi.org/10.1002/polc.5070430124.

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12

Gorbunov, A. A., and A. M. Skvortsov. "Separating power of gel permeation chromatography." Polymer Science U.S.S.R. 32, no. 3 (January 1990): 567–74. http://dx.doi.org/10.1016/0032-3950(90)90148-y.

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13

Zielinska, K., A. G. Shostenko, and S. Truszkowski. "Analysis of chitosan by gel permeation chromatography." High Energy Chemistry 48, no. 2 (March 2014): 72–75. http://dx.doi.org/10.1134/s0018143914020143.

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14

Marson, Guilherme Andrade, and Bayardo Baptista Torres. "Principles of Gel Permeation Chromatography: Interactive Software." Journal of Chemical Education 83, no. 10 (October 2006): 1567. http://dx.doi.org/10.1021/ed083p1567.2.

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15

Fu, K., Y. J. Zhang, Z. Guo, J. Wright, and Y. P. Sun. "Gel Permeation Chromatography of Fullerene-Centered Macromolecules." Journal of Chromatographic Science 42, no. 2 (February 1, 2004): 67–69. http://dx.doi.org/10.1093/chromsci/42.2.67.

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16

Boborodea, Adrian, and Stephen O'Donohue. "Low solvent consumption gel permeation chromatography method." International Journal of Polymer Analysis and Characterization 21, no. 8 (June 17, 2016): 657–62. http://dx.doi.org/10.1080/1023666x.2016.1194625.

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17

Lesec, James, and Gisele Volet. "Data treatment in multidetection gel permeation chromatography." Journal of Applied Polymer Science 45 (1990): 177–89. http://dx.doi.org/10.1002/app.1990.070450010.

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18

Chuang, Jau-Yi, Anthony R. Cooper, and Julian F. Johnson. "Gel permeation chromatography: Efficiency and operational variables." Journal of Polymer Science: Polymer Symposia 43, no. 1 (March 8, 2007): 291–97. http://dx.doi.org/10.1002/polc.5070430125.

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19

Grubisic, Z., P. Rempp, and H. Benoit. "A universal calibration for gel permeation chromatography." Journal of Polymer Science Part B: Polymer Physics 34, no. 10 (July 30, 1996): 1707–13. http://dx.doi.org/10.1002/polb.1996.922.

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20

Vilímková, Lenka, Jan Páca, Veronika Kremláčková, Jan Páca, and Marie Stiborová. "Isolation of cytoplasmic NADPH-dependent phenol hydroxylase and catechol-1,2-dioxygenase from Candida tropicalis yeast." Interdisciplinary Toxicology 1, no. 3-4 (September 1, 2008): 225–30. http://dx.doi.org/10.2478/v10102-010-0046-7.

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Isolation of cytoplasmic NADPH-dependent phenol hydroxylase and catechol-1,2-dioxygenase fromCandida tropicalisyeastThe efficiencies of NADPH-dependent phenol hydroxylase (EC 1.14.13.7) and catechol 1,2-dioxygenase (EC.1.13.11.1) in biodegradation of phenol in the cytosolic fraction isolated from yeastCandida tropicaliswere investigated. Enzymatic activities of both NADPH-dependent phenol hydroxylase and catechol 1,2-dioxygenase were detected in the cytosolic fraction ofC. tropicalisgrown on medium containing phenol. Using the procedure consisting of chromatography on DEAE-Sepharose, fractionation by polyethylene glycol 6000 and gel permeation chromatography on Sepharose 4B the enzyme responsible for phenol hydroxylation in cytosol, NADPH-dependent phenol hydroxylase, was isolated from the cytosolic fraction ofC. tropicalisclose to homogeneity. However, fractionation with polyethylene glycol 6000 lead to a decrease in catechol 1,2-dioxygenase activity. Therefore, another procedure was tested to purify this enzyme. Gel permeation chromatography of proteins of the eluate obtained by chromatography on a DEAE-Sepharose column was utilized to separate phenol hydroxylase and catechol 1,2-dioxygenase. Among gel permeation chromatography on columns of Sephadex G-100, Sephacryl S-300 and Sepharose 4B tested for their efficiencies to isolate phenol hydroxylase and catechol 1,2-dioxygenase, that on Sephacryl S-300 was found to be suitable for such a procedure. Nevertheless, even this chromatographic method did not lead to obtain catechol 1,2-dioxygenase in sufficient amounts and purity for its further characterization. The data demonstrate the progress in resolving the enzymes responsible for the first two steps of phenol degradation by theC. tropicalisstrain.
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21

Hunt, Barry J. "New directions in chromatography. New directions in gel permeation chromatography." Analytical Proceedings 30, no. 8 (1993): 338. http://dx.doi.org/10.1039/ap9933000338.

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22

Seedevi, Palaniappan, Abirami Ramu Ganesan, Kannan Mohan, Vasantharaja Raguraman, Murugesan Sivakumar, Palaniappan Sivasankar, Sivakumar Loganathan, Palasundaram Rajamalar, Shanmugam Vairamani, and Annaian Shanmugam. "Chemical structure and biological properties of a polysaccharide isolated from Pleurotus sajor-caju." RSC Advances 9, no. 35 (2019): 20472–82. http://dx.doi.org/10.1039/c9ra02977j.

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23

CHOLINSKA, MARIOLA, ZBIGNIEW DOBKOWSKI, and ALICJA KASZUBA. "Molecular characterization of polymers by gel permeation chromatography." Polimery 37, no. 11/12 (November 1992): 508–11. http://dx.doi.org/10.14314/polimery.1992.508.

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24

Coleman, William F., and Edward W. Fedosky. "A Gel Permeation Chromatography Simulator from JCE WebWare." Journal of Chemical Education 83, no. 10 (October 2006): 1567. http://dx.doi.org/10.1021/ed083p1567.1.

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25

Shansky, Richard E., and Robert E. Kane. "Separation of soy lecithin using gel permeation chromatography." Journal of Chromatography A 589, no. 1-2 (January 1992): 165–70. http://dx.doi.org/10.1016/0021-9673(92)80018-p.

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26

Terbojevich, Maria, Alessandro Cosani, Bonaventura Focher, and Enrico Marsano. "High-performance gel-permeation chromatography of chitosan samples." Carbohydrate Research 250, no. 2 (December 1993): 301–14. http://dx.doi.org/10.1016/0008-6215(93)84008-t.

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27

Newland, P., B. Bingham, E. Tarelli, and A. H. Thomas. "High-performance gel permeation chromatography of meningococcal polysaccharides." Journal of Chromatography A 483 (January 1989): 406–12. http://dx.doi.org/10.1016/s0021-9673(01)93142-5.

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28

Tennikov, M. B., A. A. Gorbunov, and A. M. Skvortsov. "Determination of polymer polydispersity by gel permeation chromatography." Journal of Chromatography A 509, no. 1 (June 1990): 219–26. http://dx.doi.org/10.1016/s0021-9673(01)93256-x.

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29

Cacace, Marcello G., Matteo Santin, and Alfonso Sada. "Behaviour of amino acids in gel permeation chromatography." Journal of Chromatography A 510 (June 1990): 41–46. http://dx.doi.org/10.1016/s0021-9673(01)93736-7.

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30

Wang, Qingguo, and Rongshi Cheng. "Evaluation of preferential solvation by gel permeation chromatography." Polymer 33, no. 18 (September 1992): 3978–80. http://dx.doi.org/10.1016/0032-3861(92)90394-c.

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31

Striegel, Andre M., and Judy D. Timpa. "Gel Permeation Chromatography of Polysaccharides Using Universal Calibration." International Journal of Polymer Analysis and Characterization 2, no. 3 (April 1996): 213–20. http://dx.doi.org/10.1080/10236669608233911.

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32

Nguyen, Tuan Q. "Kinetics of mechanochemical degradation by gel permeation chromatography." Polymer Degradation and Stability 46, no. 1 (January 1994): 99–111. http://dx.doi.org/10.1016/0141-3910(94)90114-7.

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33

Luo, Yun-Zhu, N. Kausalya Reddy, Frank Heatley, Colin Booth, Elizabeth J. Goodwin, and David Jackson. "Gel permeation chromatography of oxyethylene/oxypropylene block copolymers." European Polymer Journal 24, no. 7 (January 1988): 607–10. http://dx.doi.org/10.1016/0014-3057(88)90022-5.

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34

Schwald, Wolfgang, and Ortwin Bobleter. "Characterization of nonderivatized cellulose by gel permeation chromatography." Journal of Applied Polymer Science 35, no. 7 (May 20, 1988): 1937–44. http://dx.doi.org/10.1002/app.1988.070350719.

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35

Law, Ronald D. "Characterization of HB polymer with gel permeation chromatography." Journal of Polymer Science Part C: Polymer Symposia 21, no. 1 (March 8, 2007): 225–51. http://dx.doi.org/10.1002/polc.5070210122.

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36

Ogawa, Toshio, and Masakazu Sakai. "Gel permeation chromatography of polyamide by N-trifluoroacetylation." Journal of Polymer Science Part A: Polymer Chemistry 26, no. 12 (November 1988): 3141–49. http://dx.doi.org/10.1002/pola.1988.080261201.

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37

Bantchev, Grigor B., Steven C. Cermak, Amber L. Durham, and Neil P. J. Price. "Estolide Molecular Weight Distribution via Gel Permeation Chromatography." Journal of the American Oil Chemists' Society 96, no. 4 (March 5, 2019): 365–80. http://dx.doi.org/10.1002/aocs.12165.

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38

Lambert, A. "Analysis of brake fluids by gel permeation chromatography." Journal of Applied Chemistry 20, no. 10 (May 4, 2007): 307–11. http://dx.doi.org/10.1002/jctb.5010201003.

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39

Boborodea, A. G., M. Clemens, D. Daoust, and C. Bailly. "Gel permeation chromatography calibration based on fractal geometry." Journal of Applied Polymer Science 93, no. 2 (2004): 771–77. http://dx.doi.org/10.1002/app.20550.

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40

Bahary, W. S., and M. Jilani. "Universal calibration assessment in aqueous gel permeation chromatography." Journal of Applied Polymer Science 48, no. 9 (June 5, 1993): 1531–38. http://dx.doi.org/10.1002/app.1993.070480904.

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41

Wu, Na, Bo Zhou, He Ping Yan, Shi Juan Xu, Yun Hui Long, and Wei Liu. "Determination of Hexachlorocyclohexane (HCH) in Panax notoginseng of Chinese Traditional Medicine by Gas Chromatography/Mass Spectrometry." Advanced Materials Research 830 (October 2013): 422–25. http://dx.doi.org/10.4028/www.scientific.net/amr.830.422.

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A novel method was developed for the determination of HCH in Panax Notoginseng of Chinese traditional medicine by ultrasonic extraction (UE) coupled with Gel Permeation Chromatography and Gas Chromatography/Mass spectrometry. Some important parameters that influence the extraction and purification efficiency were investigated. The optimum condition Panax Notoginseng of Chinese traditional medicine was extracted with dichloromethane about 20mL, extracting times and extracting time were one and 30min. The extracts were cleaned up by Gel Permeation Chromatography, and determined by Gas Chromatography /Mass spectrometry. Under the optimum condition, the mean recoveries of the method were 83.23%, the relative standard deviations (RSD) were 3.45%, which has been under the demand of the determination of HCH in Panax Notoginseng of Chinese traditional medicine.
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42

Generalov, E. A., and L. V. Yakovenko. "Composition and mitogenic activity of polysaccharide from Solanum tuberosum L." Биофизика 68, no. 5 (October 15, 2023): 856–62. http://dx.doi.org/10.31857/s0006302923050034.

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Solanum tuberosum polysaccharide (STP) was isolated from the water extract of Solanum tuberosum L. and purified by ion-exchange and gel-filtration chromatography. Its molecular weight was determined by using gel permeation chromatography method and high performance liquid chromatography technique and its monosaccharide composition was analyzed using high performance liquid chromatography and gas chromatography with a flame ionization detector and a capillary column. It was shown that STP was consisted of galactose (Gal) and arabinose (Ara) (37.5 and 23.5%, respectively), along with uronic acids (9.7%), glucose monosaccharide residues (15%) and proteins (no less than 9%). The molecular weight of STP was 70 kDa. The Fourier-transform infrared technique was used for structural analysis of STP. The mitogenic activity of extracted polysaccharide is comparable to that of lipopolysaccharide.
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43

FELIPE, XAVIER, and ANDREW J. R. LAW. "SHORT COMMUNICATIONS Preparative-scale fractionation of bovine, caprine and ovine whey proteins by gel permeation chromatography." Journal of Dairy Research 64, no. 3 (August 1997): 459–64. http://dx.doi.org/10.1017/s0022029997002276.

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The whey proteins of the cow, goat and sheep have previously been fractionated on an analytical scale by reversed-phase HPLC (De Frutos et al. 1992), anion-exchange FPLC (Andrews et al. 1985; Manji et al. 1985; Laezza et al. 1991) and gel permeation FPLC (Andrews et al. 1985; Hill & Kakuda, 1990). Anion-exchange and gel permeation FPLC can readily be scaled up for laboratory preparation of whey protein fractions. There is some indication, however, that anion-exchange FPLC does not give complete separation of β-lactoglobulin and α-lactalbumin from the other minor whey protein fractions (Girardet et al. 1989).In previous work it has been shown that gel permeation FPLC gives a satisfactory fractionation of the whey proteins of the cow (Law et al. 1993), goat (Law & Brown, 1994) and sheep (Law, 1995). In this paper we describe a scaled-up method of gel permeation that can be used for fairly rapid preparation or purification of four main whey protein fractions from the milks of these species.
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44

Flapper, W., P. J. van den Oetelaar, C. P. Breed, J. Steenbergen, and H. J. Hoenders. "Detection of serum proteins by high-pressure gel-permeation chromatography with low-angle laser light scattering, compared with analytical ultracentrifugation." Clinical Chemistry 32, no. 2 (February 1, 1986): 363–67. http://dx.doi.org/10.1093/clinchem/32.2.363.

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Abstract Human sera were subjected to analytical ultracentrifugation and "high-pressure" gel-permeation chromatography on a system of combined TSK Gel G5000 PW and G3000 SW columns. The chromatographic method produced remarkably superior resolution of the proteins, especially those exceeding 100 000 Da. We calculated the molecular masses of eluted fractions on the basis of their detection by low-angle laser light scattering and their differential refractive index. We discuss the results in relation to the clinical data.
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45

Wickramanayake, Palitha P., and Walter A. Aue. "A bonded polyoxyethylene phase for gas and liquid chromatography." Canadian Journal of Chemistry 64, no. 3 (March 1, 1986): 470–76. http://dx.doi.org/10.1139/v86-073.

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Bonded phases were produced by reacting 2,4,7,9-tetramethyl-5-decyne-4,7-bis(polyethyleneoxide 30 mol) ether (Surf[Formula: see text]nol® 485) with silicic supports of high and low surface area. There is circumstantial evidence (a) that the nonextractable layer is held by multiple hydrogen bonding and (b) that the synthesis of these packings involves a reaction at the crosslinking site of the surfactant. The bonded phases, with layer thicknesses between 10 and 30 Å, were tested with three chromatographic techniques. In gas–solid chromatography, the phase proved well deactivated and yielded a reduced plate height of 2.5 (using a silica gel support). In gel permeation chromatography, polyethyleneglycols eluted within the mobile-phase volume. In liquid–solid (normal-phase adsorption) chromatography, the elution pattern differed significantly from that of unmodified silica gel. In each case, high-efficiency separations were obtained. The chromatographic experiments thus demonstrated the potential usefulness of the new phase for both gas and liquid chromatography. However, it was not tested in direct comparison with conventional phases nor was its utility established by subjecting it to routine analytical use.
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46

Steinwandter, Harald. "Gas-chromatographic determination of pesticide residues after clean-up by gel-permeation chromatography and mini-silica gel-column chromatography." Fresenius' Journal of Analytical Chemistry 354, no. 2 (February 1996): 259. http://dx.doi.org/10.1007/pl00012723.

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47

Specht, Wolfgang, Sabine Pelz, and Willi Gilsbach. "Gas-chromatographic determination of pesticide residues after clean-up by gel-permeation chromatography and mini-silica gel-column chromatography." Fresenius' Journal of Analytical Chemistry 353, no. 2 (1995): 183–90. http://dx.doi.org/10.1007/bf00322956.

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48

Specht, Wolfgang, Sabine Pelz, and Willi Gilsbach. "Gas-chromatographic determination of pesticide residues after clean-up by gel-permeation chromatography and mini-silica gel-column chromatography." Analytical and Bioanalytical Chemistry 353, no. 2 (September 1, 1995): 183–90. http://dx.doi.org/10.1007/s0021653530183.

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49

Holstege, Dirk M., David L. Scharberg, Elizabeth R. Richardson, and Gregory Möller. "Multiresidue Screen for Organophosphorus Insecticides Using Gel Permeation Chromatography—Silica Gel Cleanup." Journal of AOAC INTERNATIONAL 74, no. 2 (March 1, 1991): 394–99. http://dx.doi.org/10.1093/jaoac/74.2.394.

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Abstract A multiresidue screen for quantitative determination of 43 organophosphorus insecticides In 5 g of plant and animal tissues Is described. The organophosphorus insecticides are extracted with methanol-dichloromethane (10 + 90, v/v) and cleaned up using automated gel permeation chromatography with hexane-ethyl acetate (60 + 40) eluant and in-line silica gel minicolumns. Concentrated extracts are analyzed by gas chromatography with flame photometric detection. The method recovers 43 organophosphorus insecticides in the range of 72 to 115%. Analysis of fortified bovine liver (n = 5) shows an average 95.9 ± 4.8% recovery at the 0.05 μg/g level and 93 ± 3.8% at the 0.5 μg/g level. Analysis of fortified bovine rumen content (n = 5) shows an average 98 ± 4.2% recovery at the 0.1 μg/g level and 98.7 ± 2.8% at the 1 μg/g level. Method detection limits ranged from 0.01 to 0.05 μg/g for the compounds studied using a nominal 5 gram sample.
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50

Dickenson, J. M., T. N. Huckerby, and I. A. Nieduszynski. "Two linkage-region fragments isolated from skeletal keratan sulphate contain a sulphated N-acetylglucosamine residue." Biochemical Journal 269, no. 1 (July 1, 1990): 55–59. http://dx.doi.org/10.1042/bj2690055.

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Peptido-keratan sulphate fragments were isolated from the nucleus pulposus of bovine intervertebral discs (6-year-old animals) after chondroitin ABC lyase digestion followed by digestion of A1D1 proteoglycans by diphenylcarbamoyl chloride-treated trypsin and gel-permeation chromatography on Sepharose CL-6B. Treatment of these peptido-keratan sulphate fragments with alkaline NaB3H4 yielded keratan sulphate chains with [3H]galactosaminitol end-labels, and these chains were further purified by gel-permeation chromatography on Sephadex G-50 and ion-exchange chromatography on a Pharmacia Mono-Q column in order to exclude any contamination with O-linked oligosaccharides. The chains were then treated with keratanase, and the digest was chromatographed on a Bio-Gel P-4 column followed by anion-exchange chromatography on a Nucleosil 5 SB column. Two oligosaccharides, each representing 18% of the recovered radiolabel, were examined by 500 MHz 1H-n.m.r. spectroscopy, and shown to have the following structures: [formula: see text] The structure of oligosaccharide (I) confirms the N-acetylneuraminylgalactose substitution at position 3 of N-acetylgalactosamine in the keratan sulphate-protein linkage region found by Hopwood & Robinson [(1974) Biochem. J. 141, 57-69] but additionally shows the presence of a 6-sulphated N-acetylglucosamine. Electron micro-probe analysis specifically confirmed the presence of sulphur in this sample. This sulphate ester group differentiates the keratan sulphate linkage region from similar structures derived from O-linked oligosaccharides [Lohmander, De Luca, Nilsson, Hascall, Caputo, Kimura & Heinegård (1980) J. Biol. Chem. 255, 6084-6091].
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