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Journal articles on the topic 'Polyhistidin'

Author: Grafiati

Published: 28 June 2021

Last updated: 15 February 2022

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1

Xu, Zhaohui, and Sang Yup Lee. "Display of Polyhistidine Peptides on theEscherichia coli Cell Surface by Using Outer Membrane Protein C as an Anchoring Motif." Applied and Environmental Microbiology 65, no. 11 (November 1, 1999): 5142–47. http://dx.doi.org/10.1128/aem.65.11.5142-5147.1999.

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ABSTRACT A novel cell surface display system was developed by employingEscherichia coli outer membrane protein C (OmpC) as an anchoring motif. Polyhistidine peptides consisting of up to 162 amino acids could be successfully displayed on the seventh exposed loop of OmpC. Recombinant cells displaying polyhistidine could adsorb up to 32.0 μmol of Cd2+ per g (dry weight) of cells.

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2

DePalma, Angelo. "Keeping Tabs on Polyhistidine Tags." Genetic Engineering & Biotechnology News 36, no. 5 (March 2016): 22–24. http://dx.doi.org/10.1089/gen.36.05.12.

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3

VANGURI, Vijay K., Shuxia WANG, Svetlana GODYNA, Sripriya RANGANATHAN, and Gene LIAU. "Thrombospondin-1 binds to polyhistidine with high affinity and specificity." Biochemical Journal 347, no. 2 (April 10, 2000): 469–73. http://dx.doi.org/10.1042/bj3470469.

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Thrombospondin-1 (TSP1) is a secreted trimeric glycoprotein of 450 kDa with demonstrated effects on cell growth, adhesion and migration. Its complex biological activity is attributed to its ability to bind to cell-surface receptors, growth factors and extracellular-matrix proteins. In this study, we used a 125I solid-phase binding assay to demonstrate that TSP1 binds specifically to proteins containing polyhistidine stretches. Based on studies with three different six-histidine-containing recombinant proteins, we derived an average dissociation constant of 5 nM. The binding of 125I-labelled TSP1 to these proteins was inhibited by peptides containing histidine residues, with the degree of competition being a function of the number of histidines within the peptide. Binding was not inhibited by excess histidine or imidazole, indicating that the imidazole ring is not sufficient for recognition by TSP1. Heparin was a potent inhibitor of binding with a Ki of 50 nM, suggesting that the heparin-binding domain of TSP1 may be involved in this interaction. This was confirmed by the ability of a recombinant heparin-binding domain of TSP1 to directly compete for TSP1 binding to polyhistidine-containing proteins. Affinity chromatography with a polyhistidine-containing peptide immobilized on agarose revealed that TSP1 in platelet releasates is the major polypeptide retained on the six-histidine-peptide column. We conclude that TSP1 contains a high-affinity binding site for polyhistidine and this is likely to be the molecular basis for the observed binding of TSP1 to histidine-rich glycoprotein. The possibility that other polyhistidine-containing proteins also interact with TSP1 warrants further study.

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4

Putnam, David, Alexander N. Zelikin, Vladimir A. Izumrudov, and Robert Langer. "Polyhistidine–PEG:DNA nanocomposites for gene delivery." Biomaterials 24, no. 24 (November 2003): 4425–33. http://dx.doi.org/10.1016/s0142-9612(03)00341-7.

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5

Plumptre, Charles D., Abiodun D. Ogunniyi, and James C. Paton. "Polyhistidine triad proteins of pathogenic streptococci." Trends in Microbiology 20, no. 10 (October 2012): 485–93. http://dx.doi.org/10.1016/j.tim.2012.06.004.

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6

Mateo, Cesar, Gloria Fernandez-Lorente, Benevides C. C. Pessela, Alejandro Vian, Alfonso V. Carrascosa, Jose L. Garcia, Roberto Fernandez-Lafuente, and Jose M. Guisan. "Affinity chromatography of polyhistidine tagged enzymes." Journal of Chromatography A 915, no. 1-2 (April 2001): 97–106. http://dx.doi.org/10.1016/s0021-9673(01)00626-4.

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7

Tsuji, Shoutaro, Taku Tanaka, Naomi Hirabayashi, Shintaro Kato, Joe Akitomi, Hazuki Egashira, Iwao Waga, and Takashi Ohtsu. "RNA aptamer binding to polyhistidine-tag." Biochemical and Biophysical Research Communications 386, no. 1 (August 2009): 227–31. http://dx.doi.org/10.1016/j.bbrc.2009.06.014.

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8

Efremenko, Elena, Ilya Lyagin, Yulia Votchitseva, Maria Sirotkina, and Sergey Varfolomeyev. "Polyhistidine-containing organophosphorus hydrolase with outstanding properties." Biocatalysis and Biotransformation 25, no. 1 (January 2007): 103–8. http://dx.doi.org/10.1080/10242420601141796.

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9

Tang, Quan, Dinglei Zhao, Haiyang Yang, Lijun Wang, and Xingyuan Zhang. "A pH-responsive self-healing hydrogel based on multivalent coordination of Ni2+ with polyhistidine-terminated PEG and IDA-modified oligochitosan." Journal of Materials Chemistry B 7, no. 1 (2019): 30–42. http://dx.doi.org/10.1039/c8tb02360c.

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A multivalent Ni²⁺ coordination hydrogel based on polyhistidine-terminated PEG and IDA-modified oligochitosan with enhanced neutral stability and mild-acid responsiveness is reported herein.

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10

Miller, Adriana, Dorota Dudek, Sławomir Potocki, Hanna Czapor-Irzabek, Henryk Kozłowski, and Magdalena Rowińska-Żyrek. "Pneumococcal histidine triads – involved not only in Zn2+, but also Ni2+ binding?" Metallomics 10, no. 11 (2018): 1631–37. http://dx.doi.org/10.1039/c8mt00275d.

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11

Tett, Adrian J., Steven J. Rudder, Alexandre Bourdès, Ramakrishnan Karunakaran, and Philip S. Poole. "Regulatable Vectors for Environmental Gene Expression in Alphaproteobacteria." Applied and Environmental Microbiology 78, no. 19 (July 20, 2012): 7137–40. http://dx.doi.org/10.1128/aem.01188-12.

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ABSTRACTTwo expression vectors utilizing the inducible taurine promoter (tauAp) were developed. Plasmid pLMB51 is a stable low-copy vector enabling expression in the environment andin planta. The higher copy number pLMB509 enables BD restriction-independent cloning, expression, and purification of polyhistidine-tagged proteins.

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12

Iwasaki, Takashi, Yoshihisa Tokuda, Ayaka Kotake, Hiroyuki Okada, Shuji Takeda, Tsuyoshi Kawano, and Yuji Nakayama. "Cellular uptake and in vivo distribution of polyhistidine peptides." Journal of Controlled Release 210 (July 2015): 115–24. http://dx.doi.org/10.1016/j.jconrel.2015.05.268.

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13

Wang, Guihua, Liang Wang, Yujing Han, Shuo Zhou, and Xiyun Guan. "Nanopore detection of copper ions using a polyhistidine probe." Biosensors and Bioelectronics 53 (March 2014): 453–58. http://dx.doi.org/10.1016/j.bios.2013.10.013.

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14

Li, Zhenya, and Elliott Crooke. "Functional Analysis of Affinity-Purified Polyhistidine-Tagged DnaA Protein." Protein Expression and Purification 17, no. 1 (October 1999): 41–48. http://dx.doi.org/10.1006/prep.1999.1094.

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15

Porosk, Ly, Piret Arukuusk, Kaisa Põhako, Kaido Kurrikoff, Kristina Kiisholts, Kärt Padari, Margus Pooga, and Ülo Langel. "Enhancement of siRNA transfection by the optimization of fatty acid length and histidine content in the CPP." Biomaterials Science 7, no. 10 (2019): 4363–74. http://dx.doi.org/10.1039/c9bm00688e.

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16

Döbeli, Heinz. "Polyhistidine Affinity Chromatography: From the Idea to a Method of Broad Applicability and the Pitfalls in-between." CHIMIA International Journal for Chemistry 74, no. 5 (May 27, 2020): 363–67. http://dx.doi.org/10.2533/chimia.2020.363.

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The present article recapitulates the development of the polyhistidine affinity tag purification principle. Emphasis is laid on events behind the scenes which were never published. The key concept of the method emerged in a team discussion and its further development was driven by the need of Roche in-house projects.

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17

Aryal, Baikuntha P., and David E. Benson. "Polyhistidine Fusion Proteins Can Nucleate the Growth of CdSe Nanoparticles." Bioconjugate Chemistry 18, no. 2 (March 2007): 585–89. http://dx.doi.org/10.1021/bc060277+.

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18

VANGURI, Vijay K., Shuxia WANG, Svetlana GODYNA, Sripriya RANGANATHAN, and Gene LIAU. "Thrombospondin-1 binds to polyhistidine with high affinity and specificity." Biochemical Journal 347, no. 2 (April 15, 2000): 469. http://dx.doi.org/10.1042/0264-6021:3470469.

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19

Pinkerneil, Philipp, Jörn Güldenhaupt, Klaus Gerwert, and Carsten Kötting. "Surface-Attached Polyhistidine-Tag Proteins Characterized by FTIR Difference Spectroscopy." ChemPhysChem 13, no. 11 (June 15, 2012): 2649–53. http://dx.doi.org/10.1002/cphc.201200358.

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20

Kielkopf, Clara L., William Bauer, and Ina L. Urbatsch. "Purification of Polyhistidine-Tagged Proteins by Immobilized Metal Affinity Chromatography." Cold Spring Harbor Protocols 2020, no. 6 (June 2020): pdb.prot102194. http://dx.doi.org/10.1101/pdb.prot102194.

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21

Iwasaki, Takashi, Nodoka Murakami, and Tsuyoshi Kawano. "A polylysine–polyhistidine fusion peptide for lysosome-targeted protein delivery." Biochemical and Biophysical Research Communications 533, no. 4 (December 2020): 905–12. http://dx.doi.org/10.1016/j.bbrc.2020.09.087.

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22

Waldner, Jennifer C., Steven J. Lahr, Marshall Hall Edgell, and Gary J. Pielak. "Effect of a Polyhistidine Terminal Extension on Eglin c Stability." Analytical Biochemistry 263, no. 1 (October 1998): 116–18. http://dx.doi.org/10.1006/abio.1998.2808.

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23

Tanaka, Yoshino, Yoshihiko Nanasato, Kousei Omura, Keita Endoh, Tsuyoshi Kawano, and Takashi Iwasaki. "Direct protein delivery into intact plant cells using polyhistidine peptides." Bioscience, Biotechnology, and Biochemistry 85, no. 6 (March 31, 2021): 1405–14. http://dx.doi.org/10.1093/bbb/zbab055.

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ABSTRACT Polyhistidine peptides (PHPs), sequences comprising only histidine residues (>His8), are effective cell-penetrating peptides for plant cells. Using PHP-fusion proteins, we aimed to deliver proteins into cultured plant cells from Nicotiana tabacum, Oryza sativa, and Cryptomeria japonica. Co-cultivation of cultured cells with fusion proteins combining maltose-binding protein (MBP), red fluorescent protein (RFP), and various PHPs (MBP–RFP–His8–His20) in one polypeptide showed the cellular uptake of fusion proteins in all plant cell lines. Maximum intracellular fluorescence was shown in MBP-RFP-His20. Further, adenylate cyclase (CyaA), a synthase of cyclic adenosine monophosphate (cAMP) activated by cytosolic calmodulin, was used as a reporter for protein delivery in living cells. A fusion protein combining MBP, RFP, CyaA, and His20 (MBP–RFP–CyaA–His20) was delivered into plant cells and increased intracellular fluorescence and cAMP production in all cell lines. The present study demonstrates that PHPs are effective carriers of proteins into the intracellular space of various cultured plant cells.

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24

Pavlíková, D., T. Macek, M. Macková, M. Surá, J. Száková, and P. Tlustoš. "The evaluation of cadmium, zinc and nickel accumulation ability of transgenic tobacco bearing different transgenes." Plant, Soil and Environment 50, No. 12 (December 10, 2011): 513–17. http://dx.doi.org/10.17221/4067-pse.

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Tobacco, Nicotiana tabacum L., var. Wisconsin 38 as the control (WSC), and four genetically modified lines of the same variety, were tested for Cd, Zn and Ni accumulation. Genetically modified lines of the same variety, bearing the transgene CUP1 (gene coding a yeast metallothionein), GUS (reporter gene for ß-glucuronidase), HisCUP (CUP combined with a polyhistidine tail), and HisGUS (reporter gene for ß-glucuronidase, combined with a polyhistidine tail) under a constitutive promoter, enabling it to follow the heavy metal tolerance and uptake changes as a function of the transgene present. Control and transgenic lines were tested for accumulation of risk elements on sand nutrient medium with the addition of cadmium, zinc and nickel. The results showed high Cd accumulation ability of HisCUP line. The Cd content in aboveground biomass was increased by 90% compared to the non-transformed control and Cd content in roots was decreased by 49%. Determination of Zn content in aboveground biomass did not confirm higher uptake by transgenic plants significant for phytoremediation. The Ni content was significantly increased in aboveground biomass of HisGUS construct. GUS construct introduced the ability to accumulate all investigated metals; the others accumulated only one in extended amount.

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25

Anbarasan, Sasikala, Janne Jänis, Marja Paloheimo, Mikko Laitaoja, Minna Vuolanto, Johanna Karimäki, Pirjo Vainiotalo, Matti Leisola, and Ossi Turunen. "Effect of Glycosylation and Additional Domains on the Thermostability of a Family 10 Xylanase Produced by Thermopolyspora flexuosa." Applied and Environmental Microbiology 76, no. 1 (October 23, 2009): 356–60. http://dx.doi.org/10.1128/aem.00357-09.

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ABSTRACT The effects of different structural features on the thermostability of Thermopolyspora flexuosa xylanase XYN10A were investigated. A C-terminal carbohydrate binding module had only a slight effect, whereas a polyhistidine tag increased the thermostability of XYN10A xylanase. In contrast, glycosylation at Asn26, located in an exposed loop, decreased the thermostability of the xylanase. The presence of a substrate increased stability mainly at low pH.

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26

Samuelson, Patrik, Henrik Wernérus, Malin Svedberg, and Stefan Ståhl. "Staphylococcal Surface Display of Metal-Binding Polyhistidyl Peptides." Applied and Environmental Microbiology 66, no. 3 (March 1, 2000): 1243–48. http://dx.doi.org/10.1128/aem.66.3.1243-1248.2000.

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ABSTRACT Recombinant Staphylococcus xylosus andStaphylococcus carnosus strains were generated with surface-exposed chimeric proteins containing polyhistidyl peptides designed for binding to divalent metal ions. Surface accessibility of the chimeric surface proteins was demonstrated and the chimeric surface proteins were found to be functional in terms of metal binding, since the recombinant staphylococcal cells were shown to have gained Ni2+- and Cd2+-binding capacity, suggesting that such bacteria could find use in bioremediation of heavy metals. This is, to our knowledge, the first time that recombinant, surface-exposed metal-binding peptides have been expressed on gram-positive bacteria. Potential environmental or biosensor applications for such recombinant staphylococci as biosorbents are discussed.

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27

Torres-González, Lisa, Ramonita Díaz-Ayala, Carmen Vega-Olivencia, and Juan López-Garriga. "Characterization of Recombinant His-Tag Protein Immobilized onto Functionalized Gold Nanoparticles." Sensors 18, no. 12 (December 4, 2018): 4262. http://dx.doi.org/10.3390/s18124262.

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The recombinant polyhistidine-tagged hemoglobin I ((His)6-rHbI) from the bivalve Lucina pectinata is an ideal biocomponent for a hydrogen sulfide (H2S) biosensor due to its high affinity for H2S. In this work, we immobilized (His)6-rHbI over a surface modified with gold nanoparticles functionalized with 3-mercaptopropionic acid complexed with nickel ion. The attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) analysis of the modified-gold electrode displays amide I and amide II bands characteristic of a primarily α-helix structure verifying the presence of (His)6-rHbI on the electrode surface. Also, X-ray photoelectron spectroscopy (XPS) results show a new peak after protein interaction corresponding to nitrogen and a calculated overlayer thickness of 5.3 nm. The functionality of the immobilized hemoprotein was established by direct current potential amperometry, using H2S as the analyte, validating its activity after immobilization. The current response to H2S concentrations was monitored over time giving a linear relationship from 30 to 700 nM with a corresponding sensitivity of 3.22 × 10−3 nA/nM. These results confirm that the analyzed gold nanostructured platform provides an efficient and strong link for polyhistidine-tag protein immobilization over gold and glassy carbon surfaces for a future biosensors development.

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28

Booth, William T., Caleb R. Schlachter, Swanandi Pote, Nikita Ussin, Nicholas J. Mank, Vincent Klapper, Lesa R. Offermann, Chuanbing Tang, Barry K. Hurlburt, and Maksymilian Chruszcz. "Impact of an N-terminal Polyhistidine Tag on Protein Thermal Stability." ACS Omega 3, no. 1 (January 22, 2018): 760–68. http://dx.doi.org/10.1021/acsomega.7b01598.

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29

Thakur, Avinash Kumar, Motahareh Ghahari Larimi, Kristin Gooden, and Liviu Movileanu. "Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores." Biochemistry 56, no. 36 (August 28, 2017): 4895–905. http://dx.doi.org/10.1021/acs.biochem.7b00577.

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30

Olin, Magnus, Jonas Carlsson, and Leif Bülow. "Quantitation of Transition Metals Using Genetically Engineered Enzymes Carrying Polyhistidine Tails." Analytical Letters 28, no. 7 (May 1995): 1159–71. http://dx.doi.org/10.1080/00032719508000335.

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31

Carlsson, Jonas, Klaus Mosbach, and Leif Bülow. "Affinity precipitation and site-specific immobilization of proteins carrying polyhistidine tails." Biotechnology and Bioengineering 51, no. 2 (July 20, 1996): 221–28. http://dx.doi.org/10.1002/(sici)1097-0290(19960720)51:2<221::aid-bit12>3.0.co;2-p.

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32

LILIUS, Gosta, Mats PERSSON, Leif BULOW, and Klaus MOSBACH. "Metal affinity precipitation of proteins carrying genetically attached polyhistidine affinity tails." European Journal of Biochemistry 198, no. 2 (June 1991): 499–504. http://dx.doi.org/10.1111/j.1432-1033.1991.tb16042.x.

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33

Alessandrini, Andrea, Carlo Augusto Bortolotti, Giovanni Bertoni, Alessandro Vezzoli, and Paolo Facci. "Ultraflat Nickel Substrates for Scanning Probe Microscopy of Polyhistidine-Tagged Proteins." Journal of Physical Chemistry C 112, no. 10 (March 2008): 3747–50. http://dx.doi.org/10.1021/jp0771623.

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34

Wątły, Joanna, Aleksandra Hecel, Magdalena Rowińska-Żyrek, and Henryk Kozłowski. "Impact of histidine spacing on modified polyhistidine tag – Metal ion interactions." Inorganica Chimica Acta 472 (March 2018): 119–26. http://dx.doi.org/10.1016/j.ica.2017.06.053.

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35

Hayashi, Taiki, Matsumi Shinagawa, Tsuyoshi Kawano, and Takashi Iwasaki. "Drug delivery using polyhistidine peptide-modified liposomes that target endogenous lysosome." Biochemical and Biophysical Research Communications 501, no. 3 (June 2018): 648–53. http://dx.doi.org/10.1016/j.bbrc.2018.05.037.

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36

Kaeswurm, Julia A. H., Bettina Nestl, Sven M. Richter, Max Emperle, and Maria Buchweitz. "Purification and Characterization of Recombinant Expressed Apple Allergen Mal d 1." Methods and Protocols 4, no. 1 (December 27, 2020): 3. http://dx.doi.org/10.3390/mps4010003.

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Mal d 1 is the primary apple allergen in northern Europe. To explain the differences in the allergenicity of apple varieties, it is essential to study its properties and interaction with other phytochemicals, which might modulate the allergenic potential. Therefore, an optimized production route followed by an unsophisticated purification step for Mal d 1 and respective mutants is desired to produce sufficient amounts. We describe a procedure for the transformation of the plasmid in competent E. coli cells, protein expression and rapid one-step purification. r-Mal d 1 with and without a polyhistidine-tag are purified by immobilized metal ion affinity chromatography (IMAC) and fast-protein liquid chromatography (FPLC) using a high-resolution anion-exchange column, respectively. Purity is estimated by SDS-PAGE using an image-processing program (Fiji). For both mutants an appropriate yield of r-Mal d 1 with purity higher than 85% is achieved. The allergen is characterized after tryptic in gel digestion by peptide analyses using HPLC-MS/MS. Secondary structure elements are calculated based on CD-spectroscopy and the negligible impact of the polyhistidine-tag on the folding is confirmed. The formation of dimers is proved by mass spectrometry and reduction by DTT prior to SDS-PAGE. Furthermore, the impact of the freeze and thawing process, freeze drying and storage on dimer formation is investigated.

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37

Lee, Chang-Won, Yeon-Gil Choi, Amer Alam, and Jae-Sung Woo. "Rapid purification of HRV3C and TEV proteases using polyhistidine and polylysine tags." Korean Society for Structural Biology 8, no. 2 (June 30, 2020): 49–53. http://dx.doi.org/10.34184/kssb.2020.8.2.49.

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38

Mohanty, Arun K., and Michael C. Wiener. "Membrane protein expression and production: effects of polyhistidine tag length and position." Protein Expression and Purification 33, no. 2 (February 2004): 311–25. http://dx.doi.org/10.1016/j.pep.2003.10.010.

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39

Hwang, Seon-Kap, Peter R. Salamone, Halil Kavakli, Casey J. Slattery, and Thomas W. Okita. "Rapid purification of the potato ADP–glucose pyrophosphorylase by polyhistidine-mediated chromatography." Protein Expression and Purification 38, no. 1 (November 2004): 99–107. http://dx.doi.org/10.1016/j.pep.2004.07.018.

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40

Rodrı́guez-Dı́az, Jesús, Pilar López-Andújar, Ana Garcı́a-Dı́az, Javier Cuenca, Rebeca Montava, and Javier Buesa. "Expression and purification of polyhistidine-tagged rotavirus NSP4 proteins in insect cells." Protein Expression and Purification 31, no. 2 (October 2003): 207–12. http://dx.doi.org/10.1016/s1046-5928(03)00166-9.

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41

Liu, Jia-Wei, Ting Yang, Lin-Yu Ma, Xu-Wei Chen, and Jian-Hua Wang. "Nickel nanoparticle decorated graphene for highly selective isolation of polyhistidine-tagged proteins." Nanotechnology 24, no. 50 (November 22, 2013): 505704. http://dx.doi.org/10.1088/0957-4484/24/50/505704.

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42

Vargová, Veronika, Marko Zivanović, Vlastimil Dorčák, Emil Paleček, and Veronika Ostatná. "Catalysis of Hydrogen Evolution by Polylysine, Polyarginine and Polyhistidine at Mercury Electrodes." Electroanalysis 25, no. 9 (July 26, 2013): 2130–35. http://dx.doi.org/10.1002/elan.201300170.

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43

Plumptre, Charles D., Abiodun D. Ogunniyi, and James C. Paton. "Vaccination against Streptococcus pneumoniae Using Truncated Derivatives of Polyhistidine Triad Protein D." PLoS ONE 8, no. 10 (October 31, 2013): e78916. http://dx.doi.org/10.1371/journal.pone.0078916.

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44

Krishnani, Kishore K., Wilfred Chen, and Ashok Mulchandani. "Bactericidal activity of elastin-like polypeptide biopolymer with polyhistidine domain and silver." Colloids and Surfaces B: Biointerfaces 119 (July 2014): 66–70. http://dx.doi.org/10.1016/j.colsurfb.2014.03.018.

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45

Brown, L�cia Y., Susan E. Hodge, William G. Johnson, Sandra G. Guy, Jeffrey S. Nye, and Stephen Brown. "Possible association of NTDs with a polyhistidine tract polymorphism in theZIC2 gene." American Journal of Medical Genetics 108, no. 2 (February 14, 2002): 128–31. http://dx.doi.org/10.1002/ajmg.10221.

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46

Dalmasso, Pablo R., María L. Pedano, and Gustavo A. Rivas. "Dispersion of multi-wall carbon nanotubes in polyhistidine: Characterization and analytical applications." Analytica Chimica Acta 710 (January 2012): 58–64. http://dx.doi.org/10.1016/j.aca.2011.10.050.

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47

Pedersen, John, Conni Lauritzen, Mads Thorup Madsen, and Søren Weis Dahl. "Removal of N-Terminal Polyhistidine Tags from Recombinant Proteins Using Engineered Aminopeptidases." Protein Expression and Purification 15, no. 3 (April 1999): 389–400. http://dx.doi.org/10.1006/prep.1999.1038.

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48

Qiu, Gao-Feng, Hai-Yang Feng, and Keisuke Yamano. "Expression and Purification of Active Recombinant Cathepsin C (Dipeptidyl Aminopeptidase I) of Kuruma PrawnMarsupenaeus japonicusin Insect Cells." Journal of Biomedicine and Biotechnology 2009 (2009): 1–6. http://dx.doi.org/10.1155/2009/746289.

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Cathepsin C (CTSC) is a lysosomal cysteine protease belonging to the papain superfamily. Our previous study showed that CTSC precursor (zymogen) is localized exclusively in cortical rods (CRs) of mature oocyte in the kuruma prawnMarsupenaeus japonicus, suggesting that CTSC might have roles on regulating release and/or formation of a jelly layer. In this study, enzymically active CTSC of the kuruma prawn was prepared by recombinant expression in the High Five insect cell line. The recombinant enzyme with a polyhistidine tag at its C-terminus was considered to be initially secreted into the culture medium as an inactive form of zymogen, because Western blot with anti-CTSC antibody detected a 51 kDa protein corresponding to CTSC precursor. After purification by affinity chromatography on nickel-iminodiacetic acid resin, the enzyme displayed three forms of 51, 31, and 30 kDa polypeptides. All of the forms can be recognized by antiserum raised against C-terminal polyhistidine tag, indicating that the 31 and 30 kDa forms were generated from 51 kDa polypeptide by removal of a portion of the N-terminus of propeptide. Following activation at pH 5.5 and37∘Cfor 40 hours under native conditions, the recombinant CTSC (rCTSC) exhibited increased activity against the synthetic substrate Gly-Phe-β-naphthylamide and optimal pH at around 5. The purified rCTSC will be useful for further characterization of its exact physiological role on CRs release and/or formation of a jelly layer in kuruma prawn.

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Dabrowski, S., and J. Kur. "Recombinant His-tagged DNA polymerase. II. Cloning and purification of Thermus aquaticus recombinant DNA polymerase (Stoffel fragment)." Acta Biochimica Polonica 45, no. 3 (September 30, 1998): 661–67. http://dx.doi.org/10.18388/abp.1998_4204.

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Abstract:

The Stoffel DNA fragment, shortened by 12 bp from 5' end, coding for Stoffel DNA polymerase (missing 4 amino acids at N-terminus of Stoffel amino-acids sequence) from the thermophilic Thermus aquaticus (strain YT-1) was amplified, cloned and expressed in Escherichia coli. The recombinant Stoffel fragment contained a polyhistidine tag at the N-terminus (21 additional amino acids) that allowed its single-step isolation by Ni2+ affinity chromatography. The enzyme was characterized and displayed high DNA polymerase activity and thermostability evidently higher than the native Taq DNA polymerase.

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Грудинин, Михаил, Mihail Grudinin, Андрей Комиссаров, Andrey Komissarov, Алина Гусейнова, Alina Guseynova, Арам Шалджян, et al. "Generation and characterization of the VP1 recombinant protein of the chicken anemia virus." Russian veterinary journal 2019, no. 2 (April 30, 2019): 12–20. http://dx.doi.org/10.32416/article_5cd16d06b14db8.99635578.

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Abstract:

The aim of this study is to obtain a VP1 recombinant protein of the chicken anemia virus, capable of specifically detecting antibodies in the blood sera of sick chickens. Materials and methods. Cloning of a fragment of the VP1 gene of an infectious anemia virus of chickens was performed in the expression plasmids pET15b and pGEX-3T in the context of reading the polyhistidine sequence and glutathione-S-transferase, respectively. The recombinant proteins 6HIS-ΔVP1 and GST-ΔVP1 expressed in E. coli Rosetta (DE3) strains were purified by metal affinity chromatography. Amino acid sequence of recombinant proteins was confirmed by mass spectrometry. The specificity of the interaction of recombinant proteins with polyclonal antibodies was determined by ELISA. The ability of the recombinant 6HIS-ΔVP1 protein to detect antibodies in field and blood sera of SPF chickens was evaluated by indirect ELISA. To control the specificity of the antigen, the immune sera of birds for viruses of infectious bronchitis, Newcastle disease, infectious laryngotracheitis, adenoviral infection, Mycoplasma gallisepticum, and negative serum of chickens were used. Results. The recombinant VP1 protein of chicken anemia virus containing a polyhistidine tag (6HIS-∆VP1) was obtained. It was shown that this recombinant protein is able to specifically detect antibodies in the blood sera of sick chickens. Conclusion. The obtained recombinant protein 6HIS-ΔVP1 can be used to detect antibodies to the chicken anemia virus in the serum of sick chickens, and can also be considered as a potential component of vaccines against this virus.

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