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Journal articles on the topic '2 dimensional gel electrophoresis'

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Published: 4 June 2021

Last updated: 10 March 2023

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1

Lehr, Stefan, and Reiner Westermeier. "2-dimensional gel electrophoresis reloaded." Archives of Physiology and Biochemistry 119, no. 3 (July 2013): 93. http://dx.doi.org/10.3109/13813455.2013.812122.

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2

Deyl, Zdeněk. "Two dimensional gel electrophoresis of proteins: methods and applications." Journal of Chromatography B: Biomedical Sciences and Applications 377 (January 1986): 477. http://dx.doi.org/10.1016/s0378-4347(00)80814-2.

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3

Per, S. R., J. L. Abruzzo, and R. Heimer. "Analysis of immune complexes by two-dimensional gel electrophoresis." Clinical Immunology and Immunopathology 34, no. 2 (February 1985): 165–73. http://dx.doi.org/10.1016/0090-1229(85)90021-2.

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4

Acevedo, Fernando, and Zere Goitom. "Two-dimensional electrophoresis: agarose gel isotachophoresis followed by sodium dodecyl sulphate—polyacrylamide electrophoresis." Journal of Chromatography A 545, no. 2 (June 1991): 343–47. http://dx.doi.org/10.1016/s0021-9673(01)88725-2.

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5

MARULLO, OSVALDO, ALESSIO SOGGIU, and ENRICO CAPOBIANCO. "TWO-DIMENSIONAL ELECTROPHORESIS GEL IMAGES SCAN FOR DECOMPOSITION AND DEPLETION ANALYSIS." Advances in Adaptive Data Analysis 02, no. 03 (July 2010): 359–71. http://dx.doi.org/10.1142/s1793536910000525.

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Two-dimensional Electrophoresis Gel Images Scan (2dEGIS) implements a mix of computational methods for processing two-dimensional electrophoresis gel images. For advancing the analysis in case-control sample studies, a multi-component decomposition-approximation approach is presented, based on: (1) A global scan aimed to detect discriminative patterns with just a few components; (2) A more localized image scan through aggregated components; (3) The exploration of specific regions with maximal localization power. The tool 2dEGIS represents a novel unifying instrument for the computational analysis of gel images.

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6

Veeser, Stefan, Michael J. Dunn, and Guang-Zhong Yang. "Multiresolution image registration for two-dimensional gel electrophoresis." PROTEOMICS 1, no. 7 (July 2001): 856–70. http://dx.doi.org/10.1002/1615-9861(200107)1:7<856::aid-prot856>3.0.co;2-r.

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7

Parent, Jean-Guy, Richard Hogue, and Alain Asselin. "Glycoproteins, enzymatic activities, and b proteins in intercellular fluid extracts from hypersensitive Nicotiana species infected with tobacco mosaic virus." Canadian Journal of Botany 63, no. 5 (May 1, 1985): 928–31. http://dx.doi.org/10.1139/b85-123.

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Intercellular fluid b proteins from hypersensitive Nicotiana tabacum L. cv. Xanthi-nc and N. sylvestris Speg. and Comes infected with tobacco mosaic virus were compared by two-dimensional (2-D) polyacrylamide gel electrophoresis. Except for missing bands b2, b6a, b6b, and b7b, the overall 2-D electrophoretic pattern of N. sylvestris intercellular fluid proteins was similar to the one observed with 'Xanthi-nc' tobacco. Intercellular proteins were also studied by chromatography on con-canavalin A. Glycoproteins corresponding to b6a and b7a proteins of N. tabacum and the [Formula: see text] analog of N. sylvestris were identified. These proteins are probably peroxidase isozymes, as peroxidase activities with the same electrophoretic mobility were detected after polyacrylamide gel electrophoresis. No esterase activity was associated with any b protein band in gels. Esterase activities decreased upon virus infection, but accumulation of b proteins and peroxidase activities increased.

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8

Hochstrasser, D., V. Augsburger, T. Pun, D. Weber, C. Pellegrini, and A. F. Muller. ""High-resolution" mini-two-dimensional gel electrophoresis automatically run and stained in less than 6 h with small, ready-to-use slab gels." Clinical Chemistry 34, no. 1 (January 1, 1988): 166–70. http://dx.doi.org/10.1093/clinchem/34.1.166.

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Abstract Although two-dimensional (2-D) gel electrophoresis is one of the most powerful techniques for analyzing protein mixtures, its application in routine clinical laboratories is currently limited, because it is time-consuming, complex, and relatively expensive. Here we describe a method for automatically running and staining "high-resolution" mini 2-D electrophoresis gels in less than 6 h, by using "ready-to-use" slab gels and a PhastSystem electrophoresis apparatus. We present 2-D gel electrophoretograms of 25 nL of plasma, as well as their automatic computer analysis. For comparison, a conventional 2-D gel electrophoresis profile of 200 nL of a plasma sample is shown. The technique is easy to perform, highly sensitive, rapid, and potentially useful in semi-routine clinical chemistry laboratories.

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9

Righetti, Pier Giorgio, Annalisa Castagna, Ben Herbert, and Giovanni Candiano. "How to Bring the “Unseen” Proteome to the Limelight via Electrophoretic Pre-Fractionation Techniques." Bioscience Reports 25, no. 1-2 (February 4, 2005): 3–17. http://dx.doi.org/10.1007/s10540-005-2844-2.

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The present review reports a panoply of electrophoretic methods as pre-fractionation tools in proteomic investigations in preparation for mass spectrometry or two-dimensional electrophoresis map analysis. Such electrophoretic pre-fractionation protocols include all those electrokinetic methodologies which are performed in free solution, most of them relying on isoelectric focusing steps (although some approaches based on gels and granulated media are also discussed). Devices associated with electrophoretic separations are multi-chamber apparatuses, such as the multi-compartment electrolyzers equipped with either isoelectric membranes or with isoelectric beads, Off-Gel electrophoresis in a multi-cup device and the Rotofor, an instrument also based on a multi-chamber system but exploiting the conventional technique of carrier-ampholyte-focusing. Other free-flow systems, as well as miniaturized chambers, are also described.

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10

Deng, Ruixue, Zhaohui Lu, Yuanjia Chen, Lu Zhou, and Xinghua Lu. "Plasma Proteomic Analysis of Pancreatic Cancer by 2-Dimensional Gel Electrophoresis." Pancreas 34, no. 3 (April 2007): 310–17. http://dx.doi.org/10.1097/mpa.0b013e31802f2483.

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11

Jeng, Robert S., Shiyuan Yu, and Morris Wayman. "Isoenzyme and protein patterns of pentose-fermenting yeasts." Canadian Journal of Microbiology 33, no. 11 (November 1, 1987): 1017–23. http://dx.doi.org/10.1139/m87-179.

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Soluble proteins were extracted from the vegetative cells of four pentose-fermenting yeasts, Candida shehatae, Pichia stipitis, R-1, and R-2, the R strains being of uncertain taxonomy, while the other two are culture collection yeasts. Isoenzyme patterns, protein patterns, and two-dimensional polypeptide mapping of these four strains were compared by polyacrylamide gel electrophoresis. The two R strains showed great similarity in two-dimensional polypeptide mapping, the pattern of sodium dodecyl sulfate – polyacrylamide gel electrophoresis, isoelectrofocusing, and isoenzymes, and may be one species. Each of the other two yeasts had its own characteristic electrophoretic pattern. The R strains showed the presence of three alcohol dehydrogenase isoenzymes compared with one for the culture collection yeasts, as well as much higher activity of malate dehydrogenase, isocitrate dehydrogenase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase, which further the formation of pyruvate and ethanol.

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12

Cheng, Hao-Tsai, Sen-Yung Hsieh, Chang-Mu Sung, Betty Chien-Jung Pai, Nai-Jen Liu, and Carl PC Chen. "Optimizing Human Bile Preparation for Two-Dimensional Gel Electrophoresis." BioMed Research International 2016 (2016): 1–6. http://dx.doi.org/10.1155/2016/5185317.

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Aims. Bile is an important body fluid which assists in the digestion of fat and excretion of endogenous and exogenous compounds. In the present study, an improved sample preparation for human bile was established.Methods and Material. The method involved acetone precipitation followed by protein extraction using commercially available 2D Clean-Up kit. The effectiveness was evaluated by 2-dimensional electrophoresis (2DE) profiling quality, including number of protein spots and spot distribution.Results. The total protein of bile fluid in benign biliary disorders was 0.797 ± 0.465 μg/μL. The sample preparation method using acetone precipitation first followed by 2D Clean-Up kit protein extraction resulted in better quality of 2DE gel images in terms of resolution as compared with other sample preparation methods. Using this protocol, we obtained approximately 558 protein spots on the gel images and with better protein spots presentation of haptoglobin, serum albumin, serotransferrin, and transthyretin.Conclusions. Protein samples of bile prepared using acetone precipitation followed by 2D Clean-Up kit exhibited high protein resolution and significant protein profile. This optimized protein preparation protocol can effectively concentrate bile proteins, remove abundant proteins and debris, and yield clear presentation of nonabundant proteins and its isoforms on 2-dimensional electrophoresis gel images.

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13

Rogan, Peter K., Peter L. Lemkin, Amar J. S. Klar, Jagmohan Singh, and Jeffrey N. Strathern. "Two-dimensional agarose gel electrophoresis of restriction-digested genomic DNA." Methods 3, no. 2 (October 1991): 91–97. http://dx.doi.org/10.1016/s1046-2023(05)80200-2.

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14

Hirano, Hisashi, Hiroshi Kawasaki, and Hidenori Sassa. "Two-dimensional gel electrophoresis using immobilized pH gradient tube gels." Electrophoresis 21, no. 2 (January 1, 2000): 440–45. http://dx.doi.org/10.1002/(sici)1522-2683(20000101)21:2<440::aid-elps440>3.0.co;2-x.

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15

Leven, RM, PK Schick, and AZ Budzynski. "Fibrinogen biosynthesis in isolated guinea pig megakaryocytes." Blood 65, no. 2 (February 1, 1985): 501–4. http://dx.doi.org/10.1182/blood.v65.2.501.501.

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Abstract Fibrinogen synthesis was investigated in guinea pig megakaryocytes. Purified megakaryocytes were incubated with 35S-methionine in methionine-free incubation medium for 18 hours. Newly synthesized fibrinogen in megakaryocyte lysates enriched with purified carrier guinea pig fibrinogen was immunoprecipitated with a specific anti- guinea pig fibrinogen antiserum produced in rabbits. Proteins in the immunoprecipitates were analyzed with a 3.5% to 10.0% gradient polyacrylamide slab gel electrophoresis and auto-radiography. Radioactivity was detected in a protein band of 340,000 daltons. In order to verify fibrinogen synthesis, immunoprecipitate was analyzed by two-dimensional slab gel electrophoresis: (1) the first dimension separated unreduced fibrinogen using a 3.5% to 10.0% gradient gel; (2) following reduction by 2-beta-mercaptoethanol, fibrinogen chains were separated in the second dimension using a 10% gel. Alpha, beta, and gamma fibrinogen chains, which represented carrier guinea pig plasma fibrinogen, were visualized by Coomassie brilliant blue. Autoradiography identified the incorporation of radioactivity into the three fibrinogen chains. In control experiments, immunoprecipitates, produced by exposing megakaryocyte lysates to preimmune rabbit serum and goat anti-rabbit IgG, were also analyzed by the two-dimensional gel system. Radioactivity was not detected in sites corresponding to the migration of fibrinogen subunits. The study demonstrates that isolated guinea pig megakaryocytes can synthesize fibrinogen. The electrophoretic mobility of newly synthesized fibrinogen and subunits is similar to that of guinea pig plasma fibrinogen.

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16

Leven, RM, PK Schick, and AZ Budzynski. "Fibrinogen biosynthesis in isolated guinea pig megakaryocytes." Blood 65, no. 2 (February 1, 1985): 501–4. http://dx.doi.org/10.1182/blood.v65.2.501.bloodjournal652501.

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Fibrinogen synthesis was investigated in guinea pig megakaryocytes. Purified megakaryocytes were incubated with 35S-methionine in methionine-free incubation medium for 18 hours. Newly synthesized fibrinogen in megakaryocyte lysates enriched with purified carrier guinea pig fibrinogen was immunoprecipitated with a specific anti- guinea pig fibrinogen antiserum produced in rabbits. Proteins in the immunoprecipitates were analyzed with a 3.5% to 10.0% gradient polyacrylamide slab gel electrophoresis and auto-radiography. Radioactivity was detected in a protein band of 340,000 daltons. In order to verify fibrinogen synthesis, immunoprecipitate was analyzed by two-dimensional slab gel electrophoresis: (1) the first dimension separated unreduced fibrinogen using a 3.5% to 10.0% gradient gel; (2) following reduction by 2-beta-mercaptoethanol, fibrinogen chains were separated in the second dimension using a 10% gel. Alpha, beta, and gamma fibrinogen chains, which represented carrier guinea pig plasma fibrinogen, were visualized by Coomassie brilliant blue. Autoradiography identified the incorporation of radioactivity into the three fibrinogen chains. In control experiments, immunoprecipitates, produced by exposing megakaryocyte lysates to preimmune rabbit serum and goat anti-rabbit IgG, were also analyzed by the two-dimensional gel system. Radioactivity was not detected in sites corresponding to the migration of fibrinogen subunits. The study demonstrates that isolated guinea pig megakaryocytes can synthesize fibrinogen. The electrophoretic mobility of newly synthesized fibrinogen and subunits is similar to that of guinea pig plasma fibrinogen.

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17

Melis, Roberta, and Ray White. "Characterization of colonic polyps by two-dimensional gel electrophoresis." Electrophoresis 20, no. 4-5 (January 1, 1999): 1055–64. http://dx.doi.org/10.1002/(sici)1522-2683(19990101)20:4/5<1055::aid-elps1055>3.0.co;2-o.

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18

Robinson, P. J., I. Lefkovits, and K. Fischer Lindahl. "MOLECULAR COMPLEXITY OF Qa-2 ANTIGENS DEMONSTRATED BY TWO-DIMENSIONAL GEL ELECTROPHORESIS." European Journal of Immunogenetics 14, no. 2-3 (April 1987): 81–87. http://dx.doi.org/10.1111/j.1744-313x.1987.tb00366.x.

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19

Coulonval, Katia, Laurence Bockstaele, Sabine Paternot, and Pierre P. Roger. "Phosphorylations of Cyclin-dependent Kinase 2 Revisited Using Two-dimensional Gel Electrophoresis." Journal of Biological Chemistry 278, no. 52 (October 9, 2003): 52052–60. http://dx.doi.org/10.1074/jbc.m307012200.

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20

Posch, Anton, Thomas Franz, Sonja Hartwig, Birgit Knebel, Hadi Al-Hasani, Waltraud Passlack, Nancy Kunz, et al. "2D-ToGo workflow: increasing feasibility and reproducibility of 2-dimensional gel electrophoresis." Archives of Physiology and Biochemistry 119, no. 3 (May 17, 2013): 108–13. http://dx.doi.org/10.3109/13813455.2013.791699.

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21

Takano, K. J., T. Takano, Y. Yamanouchi, and Y. Katoh. "Analysis of Pressure Response of Human Cells Using 2-Dimensional Gel Electrophoresis." High Pressure Research 22, no. 3-4 (January 2002): 743–46. http://dx.doi.org/10.1080/08957950212425.

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22

Addeo, Francesco, Rosalba Mauriello, and Aldo Di Luccia. "A gel electrophoretic study of caprine casein." Journal of Dairy Research 55, no. 3 (August 1988): 413–21. http://dx.doi.org/10.1017/s0022029900028661.

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SummaryTo compare the resolving power of starch-urea gel (SUGE) and polyacrylamide-agarose gel electrophoresis (PAAGE) in caprine casein analysis, polyacrylamide gel isoelectric focusing (PAGIF) was used as reference method. The PAAGE or SUGE patterns in the first dimension were allowed to migrate by PAGIF in an orthogonal direction giving rise to two-dimensional (2-D) separations. Using this procedure, some individual bands considered to be homogeneous by SUGE or PAAGE were found to be complex mixtures of casein components. A detailed analysis of the analytical capabilities of SUGE and PAAGE was performed. Procedures based on the densitometric reading of SUGE and PAAGE patterns seemed to give inaccurate results on the quantitative composition of caprine casein. Among the electrophoretic methods assayed, the 2-D procedure gave the best resolution of casein fractions.

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23

Matsuhashi, Sachiko, Tsunehiro Mukai, and Katsuji Hori. "Determination of protein spots separated by two-dimensional polyacrylamide gel electrophoresis." Journal of Chromatography A 319 (January 1985): 79–89. http://dx.doi.org/10.1016/s0021-9673(01)90541-2.

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24

Zhang, Sheng, Ling-Ling Zhang, Kai-Kai Zhou, Yu-Jing Liu, and Zhong Zhao. "Evaluation of three types of protein extraction methods for tetraploid black locust (Robinia pseudoacacia L.) phloem tissue proteome analysis by two-dimensional electrophoresis." Analytical Methods 7, no. 3 (2015): 1008–17. http://dx.doi.org/10.1039/c4ay02038c.

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25

Azri, Wassim, Amel Ennajah, and Mai Jing. "Comparative study of six methods of protein extraction for two-dimensional gel electrophoresis of proteomic profiling in poplar stems." Canadian Journal of Plant Science 93, no. 5 (September 2013): 895–901. http://dx.doi.org/10.4141/cjps2013-113.

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Azri, W., Ennajah, A. and Jing, M. 2013. Comparative study of six methods of protein extraction for two-dimensional gel electrophoresis of proteomic profiling in poplar stems. Can. J. Plant Sci. 93: 895–901. Protein extraction is a crucial step in two-dimensional gel electrophoresis (2-DE) analysis of proteins, since it can have significant impact on both the quantity and the quality of protein detection. The present study is a comparison between six previously published protocols of protein extraction (A, B, C, D, E, and F) aiming to determine a suitable method to extract total proteins from poplar stems, a recalcitrant plant tissue. The obtained results revealed that method F (optimized method B), combining detergents (CHAPS, Triton X-100, and low sodium dodecyl sulfate amounts) and chaotropes (thiourea and urea), gave the best solution for the problem of protein solubilization. Method F enabled the detection of more than 300 spots reproducible on the 2-DE gel with pH 4–7 immobilized pH gradient strips and 12% sodium dodecyl sulfate–polyacrylamide gel electrophoresis, using silver staining. Our results suggest that Method F is expected to have excellent applications in proteomic studies of poplar stems.

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26

John, Huw A., and Ian F. Purdom. "Heterogeneity of human haptoglobin α chains detected by two-dimensional gel electrophoresis." Genetical Research 50, no. 1 (August 1987): 17–21. http://dx.doi.org/10.1017/s0016672300023284.

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SummaryThe protein spots representing the haptoglobin α1F, α1Sand α2chains in two-dimensional gels of human plasma samples representative of the six common haptoglobin phenotypes were identified by comparing their position with those of purified haptoglobin and distinguished from other spots in the vicinity by comparison with plasma with undetectably low levels of haptoglobin. Silver staining indicated that the α1Fchain was represented by one spot in subtypes 1F-1F, 1F-1S and 1F-2, the α1Schain by three spots in subtypes 1S-1S, 1F-1S and 1S-2 and the α2chain by six spots in 1F-2, 1S-2 and 2–2

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27

Hoving, Sjouke, Hans Voshol, and Jan van Oostrum. "Towards high performance two-dimensional gel electrophoresis using ultrazoom gels." Electrophoresis 21, no. 13 (July 1, 2000): 2617–21. http://dx.doi.org/10.1002/1522-2683(20000701)21:13<2617::aid-elps2617>3.0.co;2-c.

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28

Kumar, Manoj, Rajendra Singh, Anil Meena, Bhagwan S. Patidar, Rajendra Prasad, Sunil K. Chhabra, and Surendra K. Bansal. "An Improved 2-Dimensional Gel Electrophoresis Method for Resolving Human Erythrocyte Membrane Proteins." Proteomics Insights 8 (January 1, 2017): 117864181770088. http://dx.doi.org/10.1177/1178641817700880.

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The 2-dimensional gel electrophoresis (2-DE) technique is widely used for the analysis of complex protein mixtures extracted from biological samples. It is one of the most commonly used analytical techniques in proteomics to study qualitative and quantitative protein changes between different states of a cell or an organism (eg, healthy and diseased), conditionally expressed proteins, posttranslational modifications, and so on. The 2-DE technique is used for its unparalleled ability to separate thousands of proteins simultaneously. The resolution of the proteins by 2-DE largely depends on the quality of sample prepared during protein extraction which increases results in terms of reproducibility and minimizes protein modifications that may result in artifactual spots on 2-DE gels. The buffer used for the extraction and solubilization of proteins influences the quality and reproducibility of the resolution of proteins on 2-DE gel. The purification by cleanup kit is another powerful process to prevent horizontal streaking which occurs during isoelectric focusing due to the presence of contaminants such as salts, lipids, nucleic acids, and detergents. Erythrocyte membrane proteins serve as prototypes for multifunctional proteins in various erythroid and nonerythroid cells. In this study, we therefore optimized the selected major conditions of 2-DE for resolving various proteins of human erythrocyte membrane. The modification included the optimization of conditions for sample preparation, cleanup of protein sample, isoelectric focusing, equilibration, and storage of immobilized pH gradient strips, which were further carefully examined to achieve optimum conditions for improving the quality of protein spots on 2-DE gels. The present improved 2-DE analysis method enabled better detection of protein spots with higher quality and reproducibility. Therefore, the conditions established in this study may be used for the 2-DE analysis of erythrocyte membrane proteins for different diseases, which may help to identify the proteins that may serve as markers for diagnostics as well as targets for development of new therapeutic potential.

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29

Goez, Manuel Mauricio, Maria Constanza Torres-Madroñero, Sarah Röthlisberger, and Edilson Delgado-Trejos. "Preprocessing of 2-Dimensional Gel Electrophoresis Images Applied to Proteomic Analysis: A Review." Genomics, Proteomics & Bioinformatics 16, no. 1 (February 2018): 63–72. http://dx.doi.org/10.1016/j.gpb.2017.10.001.

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30

Sekhon, Simranjeet Singh, Ji-Young Ahn, Gonhyung Kim, Sung-Jin Cho, Hobaek Yoon, Jiho Min, and Yang-Hoon Kim. "Proteomic profiling of pig heart and lung samples using 2-dimensional gel electrophoresis." Toxicology and Environmental Health Sciences 7, no. 3 (September 2015): 190–93. http://dx.doi.org/10.1007/s13530-015-0237-x.

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31

Natale, Massimo, Bernardetta Maresca, Paolo Abrescia, and Enrico M. Bucci. "Image Analysis Workflow for 2-D Electrophoresis Gels Based on ImageJ." Proteomics Insights 4 (January 2011): PRI.S7971. http://dx.doi.org/10.4137/pri.s7971.

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A number of commercial software packages are currently available to perform digital two-dimensional electrophoresis (2D-GE) gel analysis. However, both the high cost of the commercial packages and the unavailability of a standard data analysis workflow, have prompted several groups to develop freeware systems to perform certain steps of gel analysis. Unfortunately, to the best of our knowledge none of them offer a package that performs all the steps envisaged in a 2D-GE gel analysis. Here we describe an ImageJ-based procedure, able to manage all the steps of a 2D-GE gel analysis. ImageJ is a free available image processing and analysis application developed by National Institutes of Health (NIH) and widely used in different life sciences fields as medical imaging, microscopy, western blotting and PAGE. Nevertheless no one has yet developed a procedure enabled to compare spots on 2D-GE gels. We collected all used ImageJ tools in a plug-in that allows us to perform the whole 2D-GE analysis. To test it, we performed a set of 2D-GE experiments on plasma samples from 9 patients victims of acute myocardial infarction and 8 controls, and we compared the results obtained by our procedure to those obtained using a widely diffuse commercial package, finding similar performances.

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32

Hampel, Ken J., and Jeremy S. Lee. "Two-dimensional pulsed-field gel electrophoresis of yeast chromosomes: evidence for triplex-mediated DNA condensation." Biochemistry and Cell Biology 71, no. 3-4 (March 1, 1993): 190–96. http://dx.doi.org/10.1139/o93-030.

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The mobility of yeast chromosomes was analysed by two-dimensional pulsed-field gel electrophoresis. The first dimension was run at pH 8.0 in a 1% agarose gel. In the second dimension the electrophoresis conditions were identical, except that the pH was lowered and ethidium, spermine, or ionic detergents were added. Any mobility changes between the two dimensions could be identified as a deviation from the diagonal. At pH 6.0 the mobility of the chromosomes increases severalfold, whereas at pH 4.5 none of the chromosomes move into the agarose gel. The pH-induced mobility changes were reversed by the addition of 2 μg/mL of ethidium or 1% lauryl sarcosine. Alternatively, spermine at 1 μM enhanced the pH-mediated mobility changes. Hysteresis was also evident, since upon lowering the pH to 4.5 and then running the gel at pH 7 the mobilities were decreased. These results are interpreted in terms of pH-mediated triplex formation which causes chromosome condensation and thus mobility shifts. The effects of pH are reversed by ethidium which destabilizes triplexes, but enhanced by spermine which favours triplex formation. Therefore, chromosomes may be capable of spontaneous condensation which is mediated by tertiary interactions between appropriate duplex DNA sequences.Key words: triplex DNA, pulsed-field gel electrophoresis, chromosome structure, DNA mobility, chromosome condensation.

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33

Jones, Andrew, Jonathan Wastling, and Ela Hunt. "Proposal for a Standard Representation of Two-Dimensional Gel Electrophoresis Data." Comparative and Functional Genomics 4, no. 5 (2003): 492–501. http://dx.doi.org/10.1002/cfg.323.

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The global analysis of proteins is now feasible due to improvements in techniques such as two-dimensional gel electrophoresis (2-DE), mass spectrometry, yeast two-hybrid systems and the development of bioinformatics applications. The experiments form the basis of proteomics, and present significant challenges in data analysis, storage and querying. We argue that a standard format for proteome data is required to enable the storage, exchange and subsequent re-analysis of large datasets. We describe the criteria that must be met for the development of a standard for proteomics. We have developed a model to represent data from 2-DE experiments, including difference gel electrophoresis along with image analysis and statistical analysis across multiple gels. This part of proteomics analysis is not represented in current proposals for proteomics standards. We are working with the Proteomics Standards Initiative to develop a model encompassing biological sample origin, experimental protocols, a number of separation techniques and mass spectrometry. The standard format will facilitate the development of central repositories of data, enabling results to be verified or re-analysed, and the correlation of results produced by different research groups using a variety of laboratory techniques.

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34

Guttman, András, Zsolt Csapo, and Dave Robbins. "Rapid two-dimensional analysis of proteins by ultra-thin layer gel electrophoresis." PROTEOMICS 2, no. 4 (April 2002): 469. http://dx.doi.org/10.1002/1615-9861(200204)2:4<469::aid-prot469>3.0.co;2-v.

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35

Ishimura, Ryuta, Ken Noda, Naka Hattori, Kunio Shiota, and Tomoya Ogawa. "Analysis of rat placental plasma membrane proteins by two-dimensional gel electrophoresis." Molecular and Cellular Endocrinology 115, no. 2 (December 1995): 149–59. http://dx.doi.org/10.1016/0303-7207(95)03682-2.

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36

Enroth, Helena, Thomas Åkerlund, Anna Sillén, and Lars Engstrand. "Clustering of Clinical Strains ofHelicobacter pylori Analyzed by Two-Dimensional Gel Electrophoresis." Clinical Diagnostic Laboratory Immunology 7, no. 2 (March 1, 2000): 301–6. http://dx.doi.org/10.1128/cdli.7.2.301-306.2000.

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ABSTRACT Strain variations of Helicobacter pylori have been tested by numerous methods and compared among different patient groups. The aim of this study was to investigate whether H. pyloriexpresses disease-specific proteins that can be detected by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). H. pylori strains isolated from duodenal ulcer, gastric cancer, and gastritis patients were analyzed. Extensive variation in spot patterns was observed between the strains, but a dendrogram analysis revealed that some strains within each disease group clustered together. Eight proteins were sequenced and found in the H. pylori genome sequence. 2-D PAGE is a useful method for studies of protein expression and for highlighting the extensive strain variation that H. pylori exhibits.

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37

Hoving, Sjouke, Bertran Gerrits, Hans Voshol, Dieter Müller, Rosalinda C. Roberts, and Jan van Oostrum. "Preparative two-dimensional gel electrophoresis at alkaline pH using narrow range immobilized pH gradients." PROTEOMICS 2, no. 2 (February 2002): 127–34. http://dx.doi.org/10.1002/1615-9861(200202)2:2<127::aid-prot127>3.0.co;2-y.

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Fivaz, Marc, Francis Vilbois, Christian Pasquali, and F. Gisou van der Goot. "Analysis of glycosyl phosphatidylinositol-anchored proteins by two-dimensional gel electrophoresis." Electrophoresis 21, no. 16 (October 1, 2000): 3351–56. http://dx.doi.org/10.1002/1522-2683(20001001)21:16<3351::aid-elps3351>3.0.co;2-k.

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Wang, Lining. "Proteomic Profile in Glomeruli of Type-2 Diabetic KKAy Mice using 2-Dimensional Differential Gel Electrophoresis." Medical Science Monitor 20 (2014): 2705–13. http://dx.doi.org/10.12659/msm.893078.

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Swatton, J. E., S. Prabakaran, N. A. Karp, K. S. Lilley, and S. Bahn. "Protein profiling of human postmortem brain using 2-dimensional fluorescence difference gel electrophoresis (2-D DIGE)." Molecular Psychiatry 9, no. 2 (January 6, 2004): 128–43. http://dx.doi.org/10.1038/sj.mp.4001475.

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Yoshikawa, Ken-ichi, Yohtaro Katagata, Shin-ichi Ansai, and Kazuo Aso. "A comparative study of keratins in several skin tumors by 2-dimensional gel electrophoresis (2-DE)." Journal of Dermatological Science 2, no. 3 (May 1991): 239. http://dx.doi.org/10.1016/0923-1811(91)90186-2.

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Felley-Bosco, Emanuela, Isabelle Demalte, Silvia Barcelo, Jean-Charles Sanchez, Denis F. Hochstrasser, Werner Schlegel, and Marc A. Reymond. "Information transfer between large and small two-dimensional polyacrylamide gel electrophoresis." Electrophoresis 20, no. 18 (December 1, 1999): 3508–13. http://dx.doi.org/10.1002/(sici)1522-2683(19991201)20:18<3508::aid-elps3508>3.0.co;2-7.

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LIANG, XU, JING-RONG WANG, KAM-WAI V. WONG, WEN LUAN HSIAO, HUA ZHOU, ZHI-HONG JIANG, KIN TING R. KAM, and LIANG LIU. "Optimization of 2-dimensional gel electrophoresis for proteomic studies of solid tumor tissue samples." Molecular Medicine Reports 9, no. 2 (November 20, 2013): 626–32. http://dx.doi.org/10.3892/mmr.2013.1815.

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Pattarakitkhomjon, S., S. Wongkham, W. Yutanawiboonchai, and C. Wongkham. "Analysis of plasma proteins derived from cholangiocar-cinoma patients using 2-dimensional gel electrophoresis." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A226. http://dx.doi.org/10.1042/bst028a226c.

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Rouquié, David, Annabelle Capt, William H. Eby, Vaithilingam Sekar, and Corinne Hérouet-Guicheney. "Investigation of endogenous soybean food allergens by using a 2-dimensional gel electrophoresis approach." Regulatory Toxicology and Pharmacology 58, no. 3 (December 2010): S47—S53. http://dx.doi.org/10.1016/j.yrtph.2010.09.013.

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Mitchell, A. M., J. Zagorski, L. Kruse, and J. A. Kline. "Enhanced Resolution of Human Plasma Proteins by Proteomic Separation and 2-Dimensional Gel Electrophoresis." Annals of Emergency Medicine 46, no. 3 (September 2005): 68. http://dx.doi.org/10.1016/j.annemergmed.2005.06.255.

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Jin, Xiaoying, Yajuan Chen, David M. Lubman, David Misek, and Samir M. Hanash. "Capillary electrophoresis/tandem mass spectrometry for analysis of proteins from two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis." Rapid Communications in Mass Spectrometry 13, no. 23 (December 15, 1999): 2327–34. http://dx.doi.org/10.1002/(sici)1097-0231(19991215)13:23<2327::aid-rcm792>3.0.co;2-2.

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Mortarino, Michele, Daniele Vigo, Giovanni Maffeo, and Severino Ronchi. "Two-dimensional polyacrylamide gel electrophoresis map of bovine ovarian fluid proteins." Electrophoresis 20, no. 4-5 (January 1, 1999): 866–69. http://dx.doi.org/10.1002/(sici)1522-2683(19990101)20:4/5<866::aid-elps866>3.0.co;2-v.

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Yan, Jun X., Rachel A. Harry, Carole Spibey, and Michael J. Dunn. "Postelectrophoretic staining of proteins separated by two-dimensional gel electrophoresis using SYPRO dyes." Electrophoresis 21, no. 17 (November 2000): 3657–65. http://dx.doi.org/10.1002/1522-2683(200011)21:17<3657::aid-elps3657>3.0.co;2-2.

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Laoudj-Chenivesse, Dalila, Philippe Marin, Rene Bennes, Emmanuel Tronel-Peyroz, and François Leterrier. "High performance two-dimensional gel electrophoresis using a wetting agent Tergitol® NP7." PROTEOMICS 2, no. 5 (May 2002): 481–85. http://dx.doi.org/10.1002/1615-9861(200205)2:5<481::aid-prot481>3.0.co;2-g.

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