Journal articles: 'Affinity labeling'

1

Ji, Tae H., and Inhae Ji. "Macromolecular affinity labeling." In Vitro Cellular & Developmental Biology 25, no. 8 (August 1989): 676–78. http://dx.doi.org/10.1007/bf02623719.

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2

Martini, C., and A. Lucacchini. "Affinity Labeling of Adenosine A1Binding Sites." Journal of Neurochemistry 49, no. 3 (September 1987): 681–84. http://dx.doi.org/10.1111/j.1471-4159.1987.tb00947.x.

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3

SWEET, FREDERICK, and GARY L. MURDOCK. "Affinity Labeling of Hormone-Specific Proteins*." Endocrine Reviews 8, no. 2 (May 1987): 154–84. http://dx.doi.org/10.1210/edrv-8-2-154.

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4

Shi, Yi Qun, Setsuo Furuyoshi, Ivo Hubacek, and Robert R. Rando. "Affinity labeling of lecithin retinol acyltransferase." Biochemistry 32, no. 12 (March 1993): 3077–80. http://dx.doi.org/10.1021/bi00063a019.

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Li, Hong-yu, Ying Liu, Kan Fang, and Koji Nakanishi. "A simple photo-affinity labeling protocol." Chemical Communications, no. 4 (1999): 365–66. http://dx.doi.org/10.1039/a809507h.

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SYVERTSEN, Christian, and John S. McKINLEY-McKEE. "Affinity Labeling of Liver Alcohol Dehydrogenase." European Journal of Biochemistry 117, no. 1 (March 3, 2005): 165–70. http://dx.doi.org/10.1111/j.1432-1033.1981.tb06316.x.

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Vinkenborg, Jan L., Günter Mayer, and Michael Famulok. "Aptamer-Based Affinity Labeling of Proteins." Angewandte Chemie International Edition 51, no. 36 (August 2, 2012): 9176–80. http://dx.doi.org/10.1002/anie.201204174.

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Takaoka, Yousuke, Yuuki Nukadzuka, and Minoru Ueda. "Reactive group-embedded affinity labeling reagent for efficient intracellular protein labeling." Bioorganic & Medicinal Chemistry 25, no. 11 (June 2017): 2888–94. http://dx.doi.org/10.1016/j.bmc.2017.02.059.

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Nakanishi, Shuichi, Hiroyuki Tanaka, Kazuhito Hioki, Kohei Yamada, and Munetaka Kunishima. "Labeling study of avidin by modular method for affinity labeling (MoAL)." Bioorganic & Medicinal Chemistry Letters 20, no. 23 (December 2010): 7050–53. http://dx.doi.org/10.1016/j.bmcl.2010.09.109.

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Rivera-Monroy, Zuly, Guenther K. Bonn, and András Guttman. "Fluorescent isotope-coded affinity tag 2: Peptide labeling and affinity capture." ELECTROPHORESIS 30, no. 7 (April 2009): 1111–18. http://dx.doi.org/10.1002/elps.200800830.

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Perfilov, Maxim M., Alexey S. Gavrikov, Konstantin A. Lukyanov, and Alexander S. Mishin. "Transient Fluorescence Labeling: Low Affinity—High Benefits." International Journal of Molecular Sciences 22, no. 21 (October 30, 2021): 11799. http://dx.doi.org/10.3390/ijms222111799.

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Fluorescent labeling is an established method for visualizing cellular structures and dynamics. The fundamental diffraction limit in image resolution was recently bypassed with the development of super-resolution microscopy. Notably, both localization microscopy and stimulated emission depletion (STED) microscopy impose tight restrictions on the physico-chemical properties of labels. One of them—the requirement for high photostability—can be satisfied by transiently interacting labels: a constant supply of transient labels from a medium replenishes the loss in the signal caused by photobleaching. Moreover, exchangeable tags are less likely to hinder the intrinsic dynamics and cellular functions of labeled molecules. Low-affinity labels may be used both for fixed and living cells in a range of nanoscopy modalities. Nevertheless, the design of optimal labeling and imaging protocols with these novel tags remains tricky. In this review, we highlight the pros and cons of a wide variety of transiently interacting labels. We further discuss the state of the art and future perspectives of low-affinity labeling methods.

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LINDNER, Anton J., Stephan J. GLASER, Christof K. BIEBRICHER, and Guido R. HARTMANN. "Self-catalysed affinity labeling of Qbeta replicase." European Journal of Biochemistry 202, no. 2 (December 1991): 249–54. http://dx.doi.org/10.1111/j.1432-1033.1991.tb16369.x.

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Sharifi, B. G., and T. C. Johnson. "Affinity labeling of the sialoglycopeptide antimitogen receptor." Journal of Biological Chemistry 262, no. 32 (November 1987): 15752–55. http://dx.doi.org/10.1016/s0021-9258(18)47792-7.

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Nakatani, Kazuhiko, Souta Horie, and Isao Saito. "Affinity Labeling of a Single Guanine Bulge." Journal of the American Chemical Society 125, no. 30 (July 2003): 8972–73. http://dx.doi.org/10.1021/ja0350740.

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15

Matsueda, Rei, Hideaki Umeyama, Rajinder N. Puri, Harlan N. Bradford, and Robert W. Colman. "Potent Affinity Labeling Peptide Inhibitors of Calpain." Chemistry Letters 19, no. 2 (February 1990): 191–94. http://dx.doi.org/10.1246/cl.1990.191.

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16

Rayford, R., D. D. Anthony, R. E. O'Neill, and W. C. Merrick. "Reductive alkylation with oxidized nucleotides. Use in affinity labeling or affinity chromatography." Journal of Biological Chemistry 260, no. 29 (December 1985): 15708–13. http://dx.doi.org/10.1016/s0021-9258(17)36316-0.

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17

Chiba, Kosuke, Yuichi Hashimoto, and Takao Yamaguchi. "Affinity Labeling with 4-Azidophthalimide (AzPI): Relation between Labeling Rate and Fluorescence Intensity." Chemical and Pharmaceutical Bulletin 65, no. 10 (2017): 994–96. http://dx.doi.org/10.1248/cpb.c17-00546.

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18

COLMAN, ROBERTA F., JEROME M. BAILEY, DIANNE L. DeCAMP, YU-CHU HUANG, and SARA H. VOLLMER. "Affinity Labeling of Adenine Nucleotide Sites in Enzymes." Annals of the New York Academy of Sciences 603, no. 1 Biological Ac (December 1990): 417–26. http://dx.doi.org/10.1111/j.1749-6632.1990.tb37690.x.

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19

Takagi, Shiro, Mikihiko Kobayashi, Tadanori Urayama, Itsuko Suzawa, Kazuo Matsuda, and Eiji Ichishima. "Affinity Labeling of Muscle Phosphorylasebwith α-Cyclodextrin-Dialdehyde." Agricultural and Biological Chemistry 52, no. 11 (November 1988): 2709–16. http://dx.doi.org/10.1080/00021369.1988.10869125.

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20

Ray, Rahul, Narasimha Swamy, Paul N. MacDonald, Swapna Ray, Mark R. Haussler, and Michael F. Holick. "Affinity Labeling of the 1,25-Dihydroxyvitamin D Receptor." Journal of Biological Chemistry 271, no. 4 (January 26, 1996): 2012–17. http://dx.doi.org/10.1074/jbc.271.4.2012.

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21

Dominici, P., G. Scholz, F. Kwok, and J. E. Churchich. "Affinity labeling of pyridoxal kinase with adenosine polyphosphopyridoxal." Journal of Biological Chemistry 263, no. 29 (October 1988): 14712–16. http://dx.doi.org/10.1016/s0021-9258(18)68095-0.

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22

Vaughan, Roxanne A., M. Laura Parnas, Jon D. Gaffaney, Margaret J. Lowe, Sara Wirtz, Anh Pham, Brian Reed, Sucharita M. Dutta, Kermit K. Murray, and Joseph B. Justice. "Affinity labeling the dopamine transporter ligand binding site." Journal of Neuroscience Methods 143, no. 1 (April 2005): 33–40. http://dx.doi.org/10.1016/j.jneumeth.2004.09.022.

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23

Yang, Ke, Amy Zuckerman, and Gavril W. Pasternak. "Affinity Labeling Mu Opioid Receptors With Novel Radioligands." Cellular and Molecular Neurobiology 25, no. 3-4 (June 2005): 759–65. http://dx.doi.org/10.1007/s10571-005-3973-7.

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24

NITTA, Yasunori, and Yukihiro ISODA. "Catalytic site of .BETA.-amylase and affinity labeling." Journal of the Japanese Society of Starch Science 36, no. 2 (1989): 77–85. http://dx.doi.org/10.5458/jag1972.36.77.

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25

Wong, Y. S., and J. C. Lagarias. "Affinity labeling of Avena phytochrome with ATP analogs." Proceedings of the National Academy of Sciences 86, no. 10 (May 1, 1989): 3469–73. http://dx.doi.org/10.1073/pnas.86.10.3469.

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26

Volke, Daniela, Mohammed Daghish, Lothar Hennig, Matthias Findeisen, Sabine Giesa, Ramona Oehme, and Peter Welzel. "On Penicillin-Binding Protein 1b Affinity-Labeling Reagents." Helvetica Chimica Acta 86, no. 12 (December 2003): 4214–32. http://dx.doi.org/10.1002/hlca.200390346.

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27

Jiang, Jiangsong, Dexing Zeng, and Shuwei Li. "Photogenerated Quinone Methides as Protein Affinity Labeling Reagents." ChemBioChem 10, no. 4 (February 5, 2009): 635–38. http://dx.doi.org/10.1002/cbic.200800700.

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28

Cheng, Bo, Qi Tang, Che Zhang, and Xing Chen. "Glycan Labeling and Analysis in Cells and In Vivo." Annual Review of Analytical Chemistry 14, no. 1 (June 5, 2021): 363–87. http://dx.doi.org/10.1146/annurev-anchem-091620-091314.

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As one of the major types of biomacromolecules in the cell, glycans play essential functional roles in various biological processes. Compared with proteins and nucleic acids, the analysis of glycans in situ has been more challenging. Herein we review recent advances in the development of methods and strategies for labeling, imaging, and profiling of glycans in cells and in vivo. Cellular glycans can be labeled by affinity-based probes, including lectin and antibody conjugates, direct chemical modification, metabolic glycan labeling, and chemoenzymatic labeling. These methods have been applied to label glycans with fluorophores, which enables the visualization and tracking of glycans in cells, tissues, and living organisms. Alternatively, labeling glycans with affinity tags has enabled the enrichment of glycoproteins for glycoproteomic profiling. Built on the glycan labeling methods, strategies enabling cell-selective and tissue-specific glycan labeling and protein-specific glycan imaging have been developed. With these methods and strategies, researchers are now better poised than ever to dissect the biological function of glycans in physiological or pathological contexts.

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29

Maldonado, H. M., and P. M. Cala. "Labeling of the Amphiuma erythrocyte K+/H+ exchanger with H2DIDS." American Journal of Physiology-Cell Physiology 267, no. 4 (October 1, 1994): C1002—C1012. http://dx.doi.org/10.1152/ajpcell.1994.267.4.c1002.

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Subsequent to swelling, the Amphiuma red blood cells lose K+, Cl-, and water until normal cell volume is restored. Net solute loss is the result of K+/H+ and Cl-/HCO3- exchangers functionally coupled through changes in pH and therefore HCO3-. Whereas the Cl-/HCO3- exchanger is constitutively active, K+/H+ actively is induced by cell swelling. The constitutive Cl-/HCO3- exchanger is inhibited by low concentrations (< 1 microM) of 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) or H2DIDS, yet the concentration of H2DIDS > 25 microM irreversibly modifies the K+/H+ exchanger in swollen cells. We exploited the volume-dependent irreversible low-affinity reaction between H2DIDS and the K+/H+ to identify the protein(s) associated with K+/H+ exchange activity. Labeling of the membrane proteins of intact cells with 3H2DIDS results in high-affinity labeling of a broad 100-kDa band, thought to be the anion exchanger. Additional swelling-dependent low-affinity labeling at 110 kDa suggests the possibility of a volume-induced population of anion exchangers. Finally, the correlation between volume-sensitive K+/H+ modification and low-affinity labeling suggests that transport activity is associated with a protein of approximately 85 kDa. Although a 55-kDa protein is also labeled, it is a less likely candidate, since label incorporation and transport modification are less well correlated than that of the 85- and 110-kDa proteins.

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30

Attiya, Said, Terrina Dickinson-Laing, John Cesarz, Raymond D. Giese, William E. Lee, David Mah, and D. Jed Harrison. "Affinity protection chromatography for efficient labeling of antibodies for use in affinity capillary electrophoresis." ELECTROPHORESIS 23, no. 5 (March 2002): 750–58. http://dx.doi.org/10.1002/1522-2683(200203)23:5<750::aid-elps750>3.0.co;2-3.

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31

Wong, Franklin C., John Boja, Beng Ho, Michael J. Kuhar, and Dean F. Wong. "Affinity Labeling of Membrane Receptors Using Tissue-Penetrating Radiations." BioMed Research International 2013 (2013): 1–7. http://dx.doi.org/10.1155/2013/503095.

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Photoaffinity labeling, a usefulin vivobiochemical tool, is limited when appliedin vivobecause of the poor tissue penetration by ultraviolet (UV) photons. This study investigates affinity labeling using tissue-penetrating radiation to overcome the tissue attenuation and irreversibly label membrane receptor proteins. Using X-ray (115 kVp) at low doses (<50 cGy or Rad), specific and irreversible binding was found on striatal dopamine transporters with 3 photoaffinity ligands for dopamine transporters, to different extents. Upon X-ray exposure (115 kVp), RTI-38 and RTI-78 ligands showed irreversible and specific binding to the dopamine transporter similar to those seen with UV exposure under other conditions. Similarly, gamma rays at higher energy (662 keV) also affect irreversible binding of photoreactive ligands to peripheral benzodiazepine receptors (by PK14105) and to the dopamine (D2) membrane receptors (by azidoclebopride), respectively. This study reports that X-ray and gamma rays induced affinity labeling of membrane receptors in a manner similar to UV with photoreactive ligands of the dopamine transporter, D2 dopamine receptor (D2R), and peripheral benzodiazepine receptor (PBDZR). It may provide specific noninvasive irreversible block or stimulation of a receptor using tissue-penetrating radiation targeting selected anatomic sites.

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32

Liu, Tianying, Tyler M. Marcinko, and Richard W. Vachet. "Protein–Ligand Affinity Determinations Using Covalent Labeling-Mass Spectrometry." Journal of the American Society for Mass Spectrometry 31, no. 7 (June 5, 2020): 1544–53. http://dx.doi.org/10.1021/jasms.0c00131.

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33

Johanson, R. A., and J. Henkin. "Affinity labeling of dihydrofolate reductase with an antifolate glyoxal." Journal of Biological Chemistry 260, no. 3 (February 1985): 1465–74. http://dx.doi.org/10.1016/s0021-9258(18)89615-6.

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34

Shirasu, Naoto, and Yasuyuki Shimohigashi. "Discriminative disulfide-bonding affinity labeling of opioid receptor subtypes." Journal of Biochemical and Biophysical Methods 49, no. 1-3 (October 2001): 587–606. http://dx.doi.org/10.1016/s0165-022x(01)00222-6.

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35

Löw, Andreas, Heinz G. Faulhammer, and Mathias Sprinzl. "Affinity labeling of GTP-binding proteins in cellular extracts." FEBS Letters 303, no. 1 (May 25, 1992): 64–68. http://dx.doi.org/10.1016/0014-5793(92)80478-y.

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36

Isozaki, Kaname, Hidehiko Fukahori, Takeshi Honda, Naoto Shirasu, Kazushi Okada, Takeru Nose, Kazuyasu Sakaguchi, and Yasuyuki Shimohigashi. "Site-directed affinity-labeling of delta opioid receptors by." International Journal of Peptide Research and Therapeutics 10, no. 5-6 (November 2003): 511–22. http://dx.doi.org/10.1007/s10989-004-2414-7.

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37

Vaz, Alfin D. N., and Guenther Schoellmann. "Affinity labeling of bovine opsin by trans-retinoyl chloromethane." Biochemical and Biophysical Research Communications 160, no. 2 (April 1989): 942–47. http://dx.doi.org/10.1016/0006-291x(89)92526-6.

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38

Swamy, Narasimha, and Rahul Ray. "Affinity Labeling of Rat Serum Vitamin D Binding Protein." Archives of Biochemistry and Biophysics 333, no. 1 (September 1996): 139–44. http://dx.doi.org/10.1006/abbi.1996.0374.

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39

Konziase, Benetode. "Synthesis of biotinylated probes of artemisinin for affinity labeling." Data in Brief 4 (September 2015): 66–74. http://dx.doi.org/10.1016/j.dib.2015.04.017.

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40

Amini, Frank, Thomas Kodadek, and Kathlynn C. Brown. "Protein Affinity Labeling Mediated by Genetically Encoded Peptide Tags." Angewandte Chemie 114, no. 2 (January 18, 2002): 366–69. http://dx.doi.org/10.1002/1521-3757(20020118)114:2<366::aid-ange366>3.0.co;2-6.

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41

FABRY, M., and D. BRANDENBURG. "ChemInform Abstract: Photoreactive Biotinylated Peptide Ligands for Affinity Labeling." ChemInform 28, no. 15 (August 4, 2010): no. http://dx.doi.org/10.1002/chin.199715315.

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42

Benhamou, N., N. Gilboa-Garber, J. Trudel, and A. Asselin. "A new lectin-gold complex for ultrastructural localization of galacturonic acids." Journal of Histochemistry & Cytochemistry 36, no. 11 (November 1988): 1403–11. http://dx.doi.org/10.1177/36.11.3049790.

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We report the development of a cytochemical affinity technique for detection of galacturonic acids at the ultrastructural level. The highly purified gonad lectin from Aplysia depilans (AGL) was tagged with colloidal gold particles and used for labeling carbohydrates in resin-embedded sections of various plant and fungal tissues. Patterns of AGL binding sites were compared to those obtained with a D-galactose-specific lectin, Ricinus communis agglutinin I. Differences in labeling patterns were noted, indicating that the lectins exhibited differential carbohydrate binding. In addition, the considerable loss of labeling over isolated wheat coleoptile walls treated for removal of pectin, after incubation with the AGL-gold complex, strongly suggested an affinity of AGL for pectic substances. A series of cytochemical controls, including sugar inhibition tests, has proven the specificity of the technique and the high affinity of AGL towards galacturonic acids. The potential value of this new lectin for ultrastructural studies on cell wall pectic substances in plant biology and pathology is demonstrated.

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43

Chen, Xi, Fu Li, and Yao-Wen Wu. "Chemical labeling of intracellular proteins via affinity conjugation and strain-promoted cycloadditions in live cells." Chemical Communications 51, no. 92 (2015): 16537–40. http://dx.doi.org/10.1039/c5cc05208d.

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44

Song, Yinan, Feng Xiong, Jianzhao Peng, Yi Man Eva Fung, Yiran Huang, and Xiaoyu Li. "Introducing aldehyde functionality to proteins using ligand-directed affinity labeling." Chemical Communications 56, no. 45 (2020): 6134–37. http://dx.doi.org/10.1039/d0cc01982h.

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45

Bendayan, M., and S. Garzon. "Protein G-gold complex: comparative evaluation with protein A-gold for high-resolution immunocytochemistry." Journal of Histochemistry & Cytochemistry 36, no. 6 (June 1988): 597–607. http://dx.doi.org/10.1177/36.6.2452843.

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We combined the protein G-gold complex with several polyclonal and monoclonal antibodies for localization of various antigenic sites. The labelings were compared with those obtained using the protein A-gold complex. The results from either the immunodot experiment or immunoelectron microscopy have demonstrated that, for rabbit and guinea pig antibodies, both protein G-gold and protein A-gold complexes label several different specific antibodies with similar efficiency. However, with antibodies raised in goats or in mice, and particularly with mouse monoclonal antibodies, protein G-gold yielded intense and specific labeling, whereas protein A-gold yielded intense and specific labeling, whereas protein A-gold was very variable; it either gave weaker signals or failed to reveal any specific site or, as with one monoclonal, both protein G and protein A gave similar results. The higher affinity and versatility of protein G over protein A, established by the immunochemical approach, was confirmed by immunocytochemistry. Because of its enhanced reactivity with monoclonal antibodies and its broader affinity for polyclonal antibodies, protein G-gold complex appears to be a better and more versatile probe for high-resolution immunocytochemistry.

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46

Saha, Subham, Thilo Hetzke, Thomas F. Prisner, and Snorri Th Sigurdsson. "Noncovalent spin-labeling of RNA: the aptamer approach." Chemical Communications 54, no. 83 (2018): 11749–52. http://dx.doi.org/10.1039/c8cc05597a.

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47

Van Obberghen-Schilling, Ellen, and Jacques Pouysségur. "Affinity labeling of high-affinity α-thrombin binding sites on the surface of hamster fibroblasts." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 847, no. 3 (December 1985): 335–43. http://dx.doi.org/10.1016/0167-4889(85)90039-4.

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48

Koshi, Yoichiro, Eiji Nakata, and Itaru Hamachi. "Lectin Functionalization by Post-Photo Affinity Labeling Modification (P-PALM)." Trends in Glycoscience and Glycotechnology 19, no. 107 (2007): 121–31. http://dx.doi.org/10.4052/tigg.19.121.

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49

Palma, Susana I. C. J., Alexandra R. Fernandes, and Ana C. A. Roque. "An affinity triggered MRI nanoprobe for pH-dependent cell labeling." RSC Advances 6, no. 114 (2016): 113503–12. http://dx.doi.org/10.1039/c6ra17217b.

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The pH-sensitive affinity pair composed by neutravidin and iminobiotin was used to develop a multilayered Magnetic Resonance Imaging (MRI) nanoprobe responsive to the acidic pH of tumor microenvironment.

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50

TAKAGI, Shiro, Mikihiko KOBAYASHI, Tadanori URAYAMA, Itsuko SUZAWA, Kazuo MATSUDA, and Eiji ICHISHIMA. "Affinity labeling of muscle phosphorylase b with .ALPHA.-cyclodextrin-dialdehyde." Agricultural and Biological Chemistry 52, no. 11 (1988): 2709–16. http://dx.doi.org/10.1271/bbb1961.52.2709.

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Journal articles on the topic 'Affinity labeling'

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