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Journal articles on the topic 'Fast protein liquid chromatography'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

Cho, A.-Young, Giyoung Kim, Jongguk Lim, Changyeun Mo, Ji-Hea Moon, SaetByeol Park, Su-Hee Park, and Aeson Om. "Separation of Staphylococcal Enterotoxin B by Fast Protein Liquid Chromatography." Food Engineering Progress 19, no. 2 (May 31, 2015): 111–16. http://dx.doi.org/10.13050/foodengprog.2015.19.2.111.

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2

TAKAHASHI, Sadao, Toshitaka TAMAI, Hirotada TAKAI, Shinta HAYASHI, Hajime MAEDA, Hiroyuki SAGE, Tsuguhiko INAKA, and Susumu MIYABO. "Lipoproteins Separation on Superose 6 Gel-Filtration Column Using Fast Protein Liquid Chromatography System." Journal of Japan Atherosclerosis Society 15, no. 5 (1987): 1179–83. http://dx.doi.org/10.5551/jat1973.15.5_1179.

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3

Chaplin, L. C. "Hydrophobic interaction fast protein liquid chromatography of milk proteins." Journal of Chromatography A 363, no. 2 (January 1986): 329–35. http://dx.doi.org/10.1016/s0021-9673(01)83753-5.

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4

RAHMAN, K., U. VOSS, P. J. NICHOLLS, and ALAN D. B. MALCOLM. "Nucleic acid purification by fast protein liquid chromatography." Biochemical Society Transactions 16, no. 3 (June 1, 1988): 368. http://dx.doi.org/10.1042/bst0160368.

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5

Leoni, Patricia, Paul Heyworth, and Anthony W. Segal. "Separation of phosphoproteins by fast protein liquid chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 527 (January 1990): 152–57. http://dx.doi.org/10.1016/s0378-4347(00)82093-9.

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6

Cattan, Alex R., and Julian Smith. "Computer control of fast protein liquid chromatography (FPLC)." Computers in Biology and Medicine 20, no. 2 (January 1990): 95–101. http://dx.doi.org/10.1016/0010-4825(90)90031-j.

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7

Grøstad, M., R. Rej, and N. E. Huseby. "Mitochondrial aspartate aminotransferase determined by "Fast Protein Liquid Chromatography"." Clinical Chemistry 36, no. 2 (February 1, 1990): 348–50. http://dx.doi.org/10.1093/clinchem/36.2.348.

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Abstract We describe an improved separation of the isoenzymes of aspartate aminotransferase (EC 2.6.1.1), based on ion-exchange chromatography. Involving the "Fast Protein Liquid Chromatography" system (Pharmacia) with a MonoQ column, this rapid, reproducible method for quantifying the mitochondrial enzyme shows good resolution and sensitivity, and results correlate well with those by an established immunochemical method.

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8

Andrews, A. T., M. D. Taylor, and A. J. Owen. "Rapid analysis of bovine milk proteins by fast protein liquid chromatography." Journal of Chromatography A 348 (January 1985): 177–85. http://dx.doi.org/10.1016/s0021-9673(01)92451-3.

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9

Sanogo, T., D. Paquet, F. Aubert, and G. Linden. "Purification of αS1-Casein by Fast Protein Liquid Chromatography." Journal of Dairy Science 72, no. 9 (September 1989): 2242–46. http://dx.doi.org/10.3168/jds.s0022-0302(89)79354-1.

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10

Ekstrand, Bo, and Lennart Björck. "Fast protein liquid chromatography of antibacterial components in milk." Journal of Chromatography A 358 (January 1986): 429–33. http://dx.doi.org/10.1016/s0021-9673(01)90357-7.

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11

Rodnina, M. V., Y. P. Semenkov, and W. Wintermeyer. "Purification of fMET-tRNAfMET by Fast Protein Liquid Chromatography." Analytical Biochemistry 219, no. 2 (June 1994): 380–81. http://dx.doi.org/10.1006/abio.1994.1282.

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12

Schütte, Horst, Werner Hummel, and Maria-Regina Kula. "Improved enzyme screening by automated fast protein liquid chromatography." Analytical Biochemistry 151, no. 2 (December 1985): 547–53. http://dx.doi.org/10.1016/0003-2697(85)90218-0.

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13

Davies, D. Thomas, and Andrew J. R. Law. "Quantitative fractionation of casein mixtures by fast protein liquid chromatography." Journal of Dairy Research 54, no. 3 (August 1987): 369–76. http://dx.doi.org/10.1017/s0022029900025541.

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SummaryAlkylation of whole casein samples by reaction with cysteamine and cystamine in a bis-tris-propane–urea buffer (pH 7·0) followed by fast protein liquid chromatography (FPLC) at 20°C on a Mono Q HR5/5 column in the same buffer and using a NaCl gradient led to good resolution of the whole casein into fractions representing (i) γ2- plus γ3-caseins, (ii) κ-caseins, (iii) β-casein, (iv) αs2-caseins and (v) αsl-caseins, together with small amounts of unidentified materials. Quantitatively the FPLC values agreed well with those for αs1-, β-, αs2- and γ2- plus γ3-caseins obtained by ion-exchange chromatography on DEAE cellulose, Whatman DE52 and with those for º-caseins obtained by gel-permeation chromatography on Sephadex G–150.

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14

Bastiras, S., and G. D. Calvert. "Purification of human plasma lipid transfer protein using fast protein liquid chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 383 (January 1986): 27–34. http://dx.doi.org/10.1016/s0378-4347(00)83437-4.

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15

Gustafsson, Jan-Gunnar, Ann-Kristin Frej, and Per Hedman. "Monitoring of protein product formation during fermentation with fast protein liquid chromatography." Biotechnology and Bioengineering 28, no. 1 (January 1986): 16–20. http://dx.doi.org/10.1002/bit.260280104.

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16

Johansson, Bo-Lennart, and Karin Isaksson. "Separation of phenylthiohydantoin-amino acids by fast protein liquid chromatography." Journal of Chromatography A 356 (January 1986): 383–92. http://dx.doi.org/10.1016/s0021-9673(00)91504-8.

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17

Debont, Tom, Paul Daenens, and Jan Tytgat. "Fast protein liquid chromatography for the purification of animal venoms." Journal of Pharmaceutical and Biomedical Analysis 14, no. 8-10 (June 1996): 1163–67. http://dx.doi.org/10.1016/s0731-7085(96)01747-5.

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18

Beilby, J. P., and C. Chin. "Alkaline phosphatase isoenzymes incompletely resolved by "Fast Protein Liquid Chromatography"." Clinical Chemistry 33, no. 12 (December 1, 1987): 2327. http://dx.doi.org/10.1093/clinchem/33.12.2327.

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19

Ernst, D., R. Vojacek, and D. Oesterhelt. "PURIFICATION OF PHYTOCHROME FROM RYE BY FAST PROTEIN LIQUID CHROMATOGRAPHY." Photochemistry and Photobiology 45, s1 (May 1987): 859–62. http://dx.doi.org/10.1111/j.1751-1097.1987.tb07896.x.

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20

Xia, Haifeng, Xionghua Jin, Puqiang Wu, and Zhiyong Zheng. "Porous ceramic/agarose composite adsorbents for fast protein liquid chromatography." Journal of Chromatography A 1223 (February 2012): 126–30. http://dx.doi.org/10.1016/j.chroma.2011.12.050.

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21

Hock, Dieter, Ulrich Schriek, Erich Fey, Wolf-Georg Forssmann, and Viktor Mutt. "Isolation of bovine cardiodilatin by fast protein liquid chromatography and reversed-phase high-performance liquid chromatography." Journal of Chromatography A 397 (June 1987): 347–53. http://dx.doi.org/10.1016/s0021-9673(01)85018-4.

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22

Van Gent, Teus, and Arie Van Tol. "Automated gel permeation chromatography of plasma lipoproteins by preparative fast protein liquid chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 525 (January 1990): 433–41. http://dx.doi.org/10.1016/s0378-4347(00)83420-9.

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23

Fuchs, Martin J., and Volker Keim. "Separation of rat pancreatic secretory proteins by cation-exchange fast protein liquid chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 576, no. 2 (May 1992): 287–95. http://dx.doi.org/10.1016/0378-4347(92)80202-2.

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24

Szczerba, Ted J., David N. Baehr, Louis J. Glunz, John A. Perry, and Michael J. Holdoway. "New packing and column for fast protein high-performance liquid chromatography." Journal of Chromatography A 458 (December 1988): 281–86. http://dx.doi.org/10.1016/s0021-9673(00)90571-5.

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25

BROWN, Eric D., Melodie G. WYNNE, Anthony J. CLARKE, and Rickey Y. YADA. "Purification of two fungal aspartic proteinases using fast protein liquid chromatography." Agricultural and Biological Chemistry 54, no. 6 (1990): 1563–65. http://dx.doi.org/10.1271/bbb1961.54.1563.

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26

Steinmetz, Armin, Véronique Clavey, Ngoc Vu-Dac, Hans Kaffarnik, and Jean-Charles Fruchart. "Purification of human apolipoprotein A-IV by fast protein liquid chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 487 (January 1989): 154–60. http://dx.doi.org/10.1016/s0378-4347(00)83018-2.

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27

Bell, David J., Malcolm D. Brightwell, William A. Neville, and Andrew West. "On-line liquid chromatography/fast-atom bombardment of protein tryptic digests." Rapid Communications in Mass Spectrometry 4, no. 3 (March 1990): 88–91. http://dx.doi.org/10.1002/rcm.1290040306.

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28

van Faassen, H., and R. Berger. "Separation of different forms of synthetase by fast protein liquid chromatography." Journal of Biochemical and Biophysical Methods 20, no. 3 (March 1990): 189–94. http://dx.doi.org/10.1016/0165-022x(90)90077-p.

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29

Brown, Eric D., Melodie G. Wynne, Anthony J. Clarke, and Rickey Y. Yada. "Purification of Two Fungal Aspartic Proteinases Using Fast Protein Liquid Chromatography." Agricultural and Biological Chemistry 54, no. 6 (June 1990): 1563–65. http://dx.doi.org/10.1080/00021369.1990.10870167.

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30

Olsson, Per-Erik, and Christer Hogstrand. "Improved separation of perch liver metallothionein by fast protein liquid chromatography." Journal of Chromatography A 402 (January 1987): 293–99. http://dx.doi.org/10.1016/0021-9673(87)80027-4.

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31

Vogelsang, E., and A. Schüttler. "Separation of clinically important haemoglobins by fast protein liquid chromatography (FPLC)." Fresenius' Zeitschrift für analytische Chemie 324, no. 3-4 (January 1986): 336. http://dx.doi.org/10.1007/bf00487973.

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32

Butler, Michael J., and Brian N. Gedge. "Purification of anhydrotetracycline oxygenase fromStreptomyces rimosus using fast protein liquid chromatography." Biotechnology Techniques 3, no. 4 (April 1989): 235–38. http://dx.doi.org/10.1007/bf01876055.

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33

Bronnenmeier, Karin, and Walter L. Staudenbauer. "Resolution of Clostridium stercorarium cellulase by fast protein liquid chromatography (FPLC)." Applied Microbiology and Biotechnology 27, no. 5-6 (February 1988): 432–36. http://dx.doi.org/10.1007/bf00451608.

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34

Choice, E., A. F. Ayyobi, P. H. Pritchard, and T. D. Madden. "Separation of Liposomes from Plasma Components Using Fast Protein Liquid Chromatography." Analytical Biochemistry 270, no. 1 (May 1999): 1–8. http://dx.doi.org/10.1006/abio.1999.4049.

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35

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 (November 1, 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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36

Wang, Fei, Yi Min, and Xindu Geng. "Fast separations of intact proteins by liquid chromatography." Journal of Separation Science 35, no. 22 (October 30, 2012): 3033–45. http://dx.doi.org/10.1002/jssc.201200339.

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37

Stiegler, Patrick, Marie-Lóuise Hartmann, and Jean-Pierre Ebel. "Rapid separation of Escherichia coli 30S ribosomal proteins by fast protein liquid chromatography (FPLC)." Biochimie 68, no. 4 (April 1986): 587–91. http://dx.doi.org/10.1016/s0300-9084(86)80204-8.

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38

Visweswariah, Sandhya S., and P. Radhakantha Adiga. "Isolation of riboflavin carrier proteins from pregnant human and umbilical cord serum: Similarities with chicken egg riboflavin carrier protein." Bioscience Reports 7, no. 7 (July 1, 1987): 563–71. http://dx.doi.org/10.1007/bf01119773.

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A riboflavin carrier protein has been purified from human pregnancy and umbilical cord sera by affinity chromatography and fast protein liquid chromatography. This protein has a similar molecular weight to the chicken egg riboflavin carrier protein and shares other physicochemical properties, such as pI and riboflavin binding characteristics, with the avian counterpart. A high degree of immunological cross-reactivity is observed between the human and avian riboflavin binding proteins indicating the extensive conservation of this protein throughout evolution.

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39

Booth, W. D., and C. A. White. "The isolation, purification and some properties of pheromaxein, the pheromonal steroid-binding protein, in porcine submaxillary glands and saliva." Journal of Endocrinology 118, no. 1 (July 1988): 47—NP. http://dx.doi.org/10.1677/joe.0.1180047.

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ABSTRACT Pheromaxein, the 16-androstene steroid-binding protein with a relative molecular mass of 15 000 was isolated in sub-milligram quantities from the submaxillary gland and saliva of the Gottingen miniature boar, after a fourfold purification involving the following methods: ultrafiltration for submaxillary gland cytosols and ethanol precipitation for saliva, Concanavalin-A-Sepharose affinity chromatography, sodium dodecyl sulphate polyacrylamide gel electrophoresis, 'Extractigel-D' affinity chromatography (to remove sodium dodecyl sulphate) and fast protein-liquid chromatography. Yields of purified pheromaxein obtained after fast protein-liquid chromatography represented 10–20% of total protein present in an ultrafiltrate of a submaxillary gland cytosol. Fast protein-liquid chromatography separated the α- and β-charge isomers of pheromaxein which were shown to have isoelectric points of 4·78 and 5·35 respectively on flat-bed isoelectric focusing. Some data are provided for the variable occurrence of the isomeric forms of pheromaxein in relation to different breeds of pig. Five 16-unsaturated steroids showed the highest binding to pheromaxein. Other steroids of the 5α- and 5β-androstane series also showed some binding to pheromaxein, i.e. 17β-hydroxy-5α-androstan-3-one (19·2%), with 5α-androstan-3-one, which has a similar urinous odour to 5α-androst-16-en-3-one, showing the greatest binding (42·6%) relative to 5α-androst-16-en-3-one (100%). J. Endocr. (1988) 118, 47–57

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40

Vedie, B., I. Myara, MA Pech, JC Maziere, C. Maziere, A. Caprani, and N. Moatti. "Fractionation of charge-modified low density lipoproteins by fast protein liquid chromatography." Journal of Lipid Research 32, no. 8 (August 1991): 1359–69. http://dx.doi.org/10.1016/s0022-2275(20)41966-2.

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41

Conder, Michael J., Young-Hee Ko, and Bruce A. McFadden. "Purification of Isocitrate Lyase fromEscherichia Coltand Watermelon using Fast Protein Liquid Chromatography." Preparative Biochemistry 18, no. 4 (December 1988): 431–42. http://dx.doi.org/10.1080/00327488808062542.

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42

Woody, M. A., and B. R. DasGupta. "Fast protein liquid chromatography of botulinum neurotoxin types A, B and E." Journal of Chromatography B: Biomedical Sciences and Applications 430 (January 1988): 279–89. http://dx.doi.org/10.1016/s0378-4347(00)83163-1.

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43

Giard-Pasquier, Catherine, and Urs Rickenbacher. "Purification of canine prolactin and growth hormone by fast protein liquid chromatography." Journal of Chromatography A 553 (August 1991): 117–21. http://dx.doi.org/10.1016/s0021-9673(01)88479-x.

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44

Huang, Li, Yan Chen, Ya Wang, Jian Pan, and Yuan Tong. "Isolation of DNA from genetically modified oils by fast protein liquid chromatography." International Journal of Food Science & Technology 45, no. 7 (June 21, 2010): 1495–98. http://dx.doi.org/10.1111/j.1365-2621.2010.02295.x.

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45

Motorin, Yu A., A. D. Wolfson, A. Yu Tsygankov, and A. F. Orlovsky. "Rapid isolation of Escherichia coli β-gatactosidase by fast protein liquid chromatography." Journal of Chromatography A 393, no. 2 (January 1987): 462–65. http://dx.doi.org/10.1016/s0021-9673(01)94246-3.

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46

Cubellis, Maria Vittoria, Gennaro Marino, Luciano Mayol, Gennaro Piccialli, and Giovanni Sannia. "Use of fast protein liquid chromatography for the purification of synthetic oligonucleotides." Journal of Chromatography A 329 (January 1985): 406–14. http://dx.doi.org/10.1016/s0021-9673(01)81948-8.

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47

Halima, El, Jrad Zeineb, Khorchani Touhami, Dary Annie, and Girardet JeanMichel. "Fast protein liquid chromatography of camel ?-lactalbumin fraction with radical scavenging activity." Emirates Journal of Food and Agriculture 26, no. 4 (2014): 309. http://dx.doi.org/10.9755/ejfa.v26i4.16178.

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48

Hollar, C. M., A. J. R. Law, D. G. Dalgleish, and R. J. Brown. "Separation of Major Casein Fractions Using Cation-Exchange Fast Protein Liquid Chromatography." Journal of Dairy Science 74, no. 8 (August 1991): 2403–9. http://dx.doi.org/10.3168/jds.s0022-0302(91)78414-2.

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49

Mokhtarian, Kobra, Lame Akhlaghi, Ahmad Reza Meamar, Elham Razmjou, Kourosh Manouchehri Naeini, Samaneh Gholami, Masoomeh Najafi Samei, and Reza Falak. "Serodiagnosis of fasciolosis by fast protein liquid chromatography-fractionated excretory/secretory antigens." Parasitology Research 115, no. 8 (April 30, 2016): 2957–65. http://dx.doi.org/10.1007/s00436-016-5049-7.

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50

Gaillard, I., A. Martial, A. Marc, J. M. Engasser, and M. Fick. "Analytical method optimization for protein determination by fast high-performance liquid chromatography." Journal of Chromatography A 679, no. 2 (September 1994): 261–68. http://dx.doi.org/10.1016/0021-9673(94)80568-7.

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