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Artículos de revistas sobre el tema "Escherichia coli Inclusions"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 1 de febrero de 2022

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1

Hänisch, Jan, Marc Wältermann, Horst Robenek, and Alexander Steinbüchel. "The Ralstonia eutropha H16 phasin PhaP1 is targeted to intracellular triacylglycerol inclusions in Rhodococcus opacus PD630 and Mycobacterium smegmatis mc2155, and provides an anchor to target other proteins." Microbiology 152, no. 11 (November 1, 2006): 3271–80. http://dx.doi.org/10.1099/mic.0.28969-0.

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In Ralstonia eutropha, the H16 phasin PhaP1 represents the major phasin that binds to the surface of polyhydroxyalkanoate (PHA) inclusions. In this study, C-terminal fusions of PhaP1 with enhanced green fluorescent protein (eGFP) and with Escherichia coli β-galactosidase (LacZ) were expressed separately in the triacylglycerol (TAG)-accumulating actinomycetes Rhodococcus opacus PD630 and Mycobacterium smegmatis mc2155, employing the M. smegmatis acetamidase (ace) promoter of the Escherichia–Mycobacterium/Rhodococcus shuttle plasmid pJAM2. PhaP1 and the PhaP1 fusion proteins were expressed stabl

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2

Chen, Shuxiong, Natalie A. Parlane, Jason Lee, D. Neil Wedlock, Bryce M. Buddle, and Bernd H. A. Rehm. "New Skin Test for Detection of Bovine Tuberculosis on the Basis of Antigen-Displaying Polyester Inclusions Produced by Recombinant Escherichia coli." Applied and Environmental Microbiology 80, no. 8 (February 14, 2014): 2526–35. http://dx.doi.org/10.1128/aem.04168-13.

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ABSTRACTThe tuberculin skin test for diagnosing tuberculosis (TB) in cattle lacks specificity if animals are sensitized to environmental mycobacteria, as some antigens in purified protein derivative (PPD) prepared fromMycobacterium bovisare present in nonpathogenic mycobacteria. Three immunodominant TB antigens, ESAT6, CFP10, and Rv3615c, are present in members of the pathogenicMycobacterium tuberculosiscomplex but absent from the majority of environmental mycobacteria. These TB antigens have the potential to enhance skin test specificity. To increase their immunogenicity, these antigens were

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3

Davis, Katelin L., Liang Cheng, José Ramos-Vara, Melissa D. Sánchez, Rebecca P. Wilkes, and Mario F. Sola. "Malakoplakia in the Urinary Bladder of 4 Puppies." Veterinary Pathology 58, no. 4 (April 23, 2021): 699–704. http://dx.doi.org/10.1177/03009858211009779.

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Malakoplakia in humans most often affects the urinary bladder and is characterized by inflammation with von Hansemann–type macrophages, with or without Michaelis-Gutmann bodies, and is frequently associated with Escherichia coli infection. We describe the microscopic features of malakoplakia in the urinary bladder of 4 puppies. In all cases, the lamina propria of the urinary bladder was markedly expanded by sheets of large, round to polygonal macrophages with intracytoplasmic, periodic acid-Schiff-positive granules and granular inclusions, and rare Prussian blue–positive inclusions. Macrophage

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4

Wada, Y., H. Kondo, Y. Nakaoka, and M. Kubo. "Gastric Attaching and Effacing Escherichia coli Lesions in a Puppy with Naturally Occurring Enteric Colibacillosis and Concurrent Canine Distemper Virus Infection." Veterinary Pathology 33, no. 6 (November 1996): 717–20. http://dx.doi.org/10.1177/030098589603300615.

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A puppy suffering from chronic diarrhea was humanely killed at 90 days of age. Numerous Gram-negative bacilli were found adhering to the surface of as well as within epithelial cells from the stomach to the colon. Canine distemper virus inclusions were in the epithelial cytoplasm of the esophageal, gastric, and intestinal mucosa. Typical attaching and effacing ultrastructural lesions were in the stomach, and some bacilli were in the cytoplasm of the epithelial cells, Escherichia coli, isolated from the contents of the small intestine, belonged to serotype 0118: NM and were negative for plasmid

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5

Aldrich, H. C., S. Elvington, HE Machines, R. Szabady, K. Feder, L. McDowell, and J. M. Shively. "Ultrastructural and Cytochemical Analyses of the Expression of the Thiobacillus Carboxysome Operon in Escherichia Coli." Microscopy and Microanalysis 7, S2 (August 2001): 740–41. http://dx.doi.org/10.1017/s1431927600029779.

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The cytoplasm of the bacterium Thiobacillus neapolitanus contains 117 nm diameter polyhedral inclusions, “carboxysomes” (Fig. 1) that contain ribulose-1,5- bisphosphate carboxylase/oxygenase (RuBisCO). Surrounding the polyhedron are nonmembranous proteinaceous plates devoid of lipid. The carboxysomes are composed of at least 8 major peptides, all coded within the same operon. Six (CsoSIA, CsoSIB, CsoSIC, CsoS2A, CsoS2B, and CsoS3) make up the shell, and two are the large (CbbL) and small subunits (CbbS) of RuBisCO. Using immunogold labeling on ultrathin sections, peptides CsoS2A, CsoS2B, and C

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6

Blatchford, Paul A., Colin Scott, Nigel French, and Bernd H. A. Rehm. "Immobilization of organophosphohydrolase OpdA from Agrobacterium radiobacter by overproduction at the surface of polyester inclusions inside engineered Escherichia coli." Biotechnology and Bioengineering 109, no. 5 (December 26, 2011): 1101–8. http://dx.doi.org/10.1002/bit.24402.

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7

Kalscheuer, Rainer, Tim Stöveken, Heinrich Luftmann, Ursula Malkus, Rudolf Reichelt, and Alexander Steinbüchel. "Neutral Lipid Biosynthesis in Engineered Escherichia coli: Jojoba Oil-Like Wax Esters and Fatty Acid Butyl Esters." Applied and Environmental Microbiology 72, no. 2 (February 2006): 1373–79. http://dx.doi.org/10.1128/aem.72.2.1373-1379.2006.

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ABSTRACT Wax esters are esters of long-chain fatty acids and long-chain fatty alcohols which are of considerable commercial importance and are produced on a scale of 3 million tons per year. The oil from the jojoba plant (Simmondsia chinensis) is the main biological source of wax esters. Although it has a multitude of potential applications, the use of jojoba oil is restricted, due to its high price. In this study, we describe the establishment of heterologous wax ester biosynthesis in a recombinant Escherichia coli strain by coexpression of a fatty alcohol-producing bifunctional acyl-coenzyme

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8

Petrus, Marloes L. C., Lukas A. Kiefer, Pranav Puri, Evert Heemskerk, Michael S. Seaman, Dan H. Barouch, Sagrario Arias, Gilles P. van Wezel, and Menzo Havenga. "A microbial expression system for high-level production of scFv HIV-neutralizing antibody fragments in Escherichia coli." Applied Microbiology and Biotechnology 103, no. 21-22 (October 22, 2019): 8875–88. http://dx.doi.org/10.1007/s00253-019-10145-1.

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Abstract Monoclonal antibodies (mABs) are of great biopharmaceutical importance for the diagnosis and treatment of diseases. However, their production in mammalian expression hosts usually requires extensive production times and is expensive. Escherichia coli has become a new platform for production of functional small antibody fragment variants. In this study, we have used a rhamnose-inducible expression system that allows precise control of protein expression levels. The system was first evaluated for the cytoplasmic production of super folder green fluorescence protein (sfGFP) in various pr

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9

Carija, Pinheiro, Iglesias, and Ventura. "Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation." Cells 8, no. 8 (August 8, 2019): 856. http://dx.doi.org/10.3390/cells8080856.

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The aggregation of proteins compromises cell fitness, either because it titrates functional proteins into non-productive inclusions or because it results in the formation of toxic assemblies. Accordingly, computational proteome-wide analyses suggest that prevention of aggregation upon misfolding plays a key role in sequence evolution. Most proteins spend their lifetimes in a folded state; therefore, it is conceivable that, in addition to sequences, protein structures would have also evolved to minimize the risk of aggregation in their natural environments. By exploiting the AGGRESCAN3D structu

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10

Rybalchenko, O. V., O. G. Orlova, L. B. Zakharova, O. N. Vishnevskaya, and A. G. Markov. "EFFECT OF PROBIOTIC BACTERIA AND LIPOPOLISACCHARIDES ON EPITELIOCYTES TIGHT JUNCTIONS OF RAT JEJUNUM." Journal of microbiology epidemiology immunobiology, no. 6 (December 28, 2017): 80–87. http://dx.doi.org/10.36233/0372-9311-2017-6-80-87.

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Aim. The present study has been undertaken with the main objective the influence of probiotic bacteria Lactobacillus plantarum 8 РАЗ and Escherichia coli M17 and lipopolysaccharide on the ultrastructure of enterocytes tight junctions of mucous membranes of rat jejunum. Materials and methods. The study was carried out on E. coli lipopolysaccharide (Sigma-Aldrich, Germany) and probiotic bacteria L. plantarum 8PA3 and E. coli M17. Male Wistar rats were used. A comparative analysis of the ultrathin structure of enterocytes and tight junctions were carried out by successive incubation of rat jejunu

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11

Kushnir, I. M., G. V. Kolodiy, V. I. Kushnir, S. D. Murska, I. S. Semen, and U. Z. Berbeka. "THE INFLUENCE OF POLYHEXAMETHYLENE GUANIDINE SALTS ON THE MICROBIOLOGICAL PARAMETERS OF WATER." Scientific and Technical Bulletin оf State Scientific Research Control Institute of Veterinary Medical Products and Fodder Additives аnd Institute of Animal Biology 22, no. 1 (March 29, 2021): 126–30. http://dx.doi.org/10.36359/scivp.2021-22-1.14.

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The article represent the use of disinfectant which was made based on salts of polyhexamethylene guanidine hydrochloride (PGMG-hydrochloride) and polyhexamethylene guanidine phosphate (PGMG-phosphate) for water disinfection. Water plays one of the most important roles in almost all life processes. Water is a part of the blood, participates in blood circulatory system, delivers nutrients and oxygen to the organs, participates in oxidation reaction, hydrolysis and other reactions of intercellular metabolism, forms an environment to maintain a healthy microflora of the digestive tract, which prov

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12

Park, Youngjin, Mohd Amir F. Abdullah, Milton D. Taylor, Khalidur Rahman, and Michael J. Adang. "Enhancement of Bacillus thuringiensis Cry3Aa and Cry3Bb Toxicities to Coleopteran Larvae by a Toxin-Binding Fragment of an Insect Cadherin." Applied and Environmental Microbiology 75, no. 10 (March 27, 2009): 3086–92. http://dx.doi.org/10.1128/aem.00268-09.

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ABSTRACT The Cry3Aa and Cry3Bb insecticidal proteins of Bacillus thuringiensis are used in biopesticides and transgenic crops to control larvae of leaf-feeding beetles and rootworms. Cadherins localized in the midgut epithelium are identified as receptors for Cry toxins in lepidopteran and dipteran larvae. Previously, we discovered that a peptide of a toxin-binding cadherin expressed in Escherichia coli functions as a synergist for Cry1A toxicity against lepidopteran larvae and Cry4 toxicity against dipteran larvae. Here we report that the fragment containing the three most C-terminal cadherin

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13

Tam, Jeffrey E., Carolyn H. Davis, and Priscilla B. Wyrick. "Expression of recombinant DNA introduced into Chlamydia trachomatis by electroporation." Canadian Journal of Microbiology 40, no. 7 (July 1, 1994): 583–91. http://dx.doi.org/10.1139/m94-093.

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Electroporation was used to introduce DNA into the elementary bodies of the obligate parasitic bacterium Chlamydia trachomatis. The source of DNA for these experiments was the chimeric plasmid pPBW100, which was constructed from the well-characterized 7.5-kb plasmid of C. trachomatis and the Escherichia coli plasmid pBGS9. To select directly for C. trachomatis carrying pPBW100, an in-frame gene fusion between the chlamydial promoter P7248 and a promoterless chloramphenicol acetyltransferase (cat) cassette was incorporated into the plasmid. After infection of McCoy cells with electroporated ele

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14

Mifune, Jun, Katrin Grage, and Bernd H. A. Rehm. "Production of Functionalized Biopolyester Granules by Recombinant Lactococcus lactis." Applied and Environmental Microbiology 75, no. 14 (May 22, 2009): 4668–75. http://dx.doi.org/10.1128/aem.00487-09.

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ABSTRACT Many bacteria are naturally capable of accumulating biopolyesters composed of 3-hydroxy fatty acids as intracellular inclusions, which serve as storage granules. Recently, these inclusions have been considered as nano-/microbeads with surface-attached proteins, which can be engineered to display various protein-based functions that are suitable for biotechnological and biomedical applications. In this study, the food-grade, generally-regarded-as-safe gram-positive organism Lactococcus lactis was engineered to recombinantly produce the biopolyester poly(3-hydroxybutyrate) and the respe

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15

Parlane, Natalie A., D. Neil Wedlock, Bryce M. Buddle, and Bernd H. A. Rehm. "Bacterial Polyester Inclusions Engineered To Display Vaccine Candidate Antigens for Use as a Novel Class of Safe and Efficient Vaccine Delivery Agents." Applied and Environmental Microbiology 75, no. 24 (October 16, 2009): 7739–44. http://dx.doi.org/10.1128/aem.01965-09.

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ABSTRACT Bioengineered bacterial polyester inclusions have the potential to be used as a vaccine delivery system. The biopolyester beads were engineered to display a fusion protein of the polyester synthase PhaC and the two key antigens involved in immune response to the infectious agent that causes tuberculosis, Mycobacterium tuberculosis, notably antigen 85A (Ag85A) and the 6-kDa early secreted antigenic target (ESAT-6) from Mycobacterium tuberculosis. Polyester beads displaying the respective fusion protein at a high density were successfully produced (henceforth called Ag85A-ESAT-6 beads)

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16

Kim, Won-Seok, Jeong Sun-Hyung, Ro-Dong Park, Kil-Yong Kim, and Hari B. Krishnan. "Sinorhizobium fredii USDA257 Releases a 22-kDa Outer Membrane Protein (Omp22) to the Extracellular Milieu When Grown in Calcium-Limiting Conditions." Molecular Plant-Microbe Interactions® 18, no. 8 (August 2005): 808–18. http://dx.doi.org/10.1094/mpmi-18-0808.

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Calcium, which regulates a wide variety of cellular functions, plays an important role in Rhizobium-legume interactions. We investigated the effect of calcium on surface appendages of Sinorhizobium fredii USDA257. Cold-field emission scanning electron microscopy observation of USDA257 grown in calcium-limiting conditions revealed cells with unusual shape and size. Transmission electron microscopy observation revealed intact flagella were present only when USDA257 cells were grown in calcium-sufficient conditions. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of flagellar p

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17

Gorbatuk, O. B., U. S. Nikolayev, D. M. Irodov, I. Ya Dubey, and P. V. Gilchuk. "Refolding of ScFv-CBD fusion protein from Escherichia coli inclusion bodies." Biopolymers and Cell 24, no. 1 (January 20, 2008): 51–59. http://dx.doi.org/10.7124/bc.000790.

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18

Steinmann, Björn, Andreas Christmann, Tim Heiseler, Janine Fritz, and Harald Kolmar. "In Vivo Enzyme Immobilization by Inclusion Body Display." Applied and Environmental Microbiology 76, no. 16 (June 25, 2010): 5563–69. http://dx.doi.org/10.1128/aem.00612-10.

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ABSTRACT A novel strategy for in vivo immobilization of enzymes on the surfaces of inclusion bodies has been established. It relies on expression in Escherichia coli of the polyhydroxybutyrate synthase PhaC from Cupriavidus necator, which carries at its amino terminus an engineered negatively charged α-helical coil (Ecoil) and forms inclusion bodies upon high-level expression. Coexpression in the same cell of galactose oxidase (GOase) from Fusarium spp. carrying a carboxy-terminal positively charged coil (lysine-rich coil [Kcoil]) sequence results in heterodimeric coiled-coil formation in vivo

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19

Johnson, Dustin L., Chris B. Stone, and James B. Mahony. "Interactions between CdsD, CdsQ, and CdsL, Three Putative Chlamydophila pneumoniae Type III Secretion Proteins." Journal of Bacteriology 190, no. 8 (February 15, 2008): 2972–80. http://dx.doi.org/10.1128/jb.01997-07.

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ABSTRACT Chlamydophila pneumoniae is a gram-negative obligate intracellular bacterial pathogen that causes pneumonia and bronchitis and may contribute to atherosclerosis. The developmental cycle of C. pneumoniae includes a morphological transition from an infectious extracellular elementary body (EB) to a noninfectious intracellular reticulate body (RB) that divides by binary fission. The C. pneumoniae genome encodes a type III secretion (T3S) apparatus that may be used to infect eukaryotic cells and to evade the host immune response. In the present study, Cpn0712 (CdsD), Cpn0704 (CdsQ), and C

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20

Tzeng, Yih-Ling, Anup K. Datta, Cristy A. Strole, Michael A. Lobritz, Russell W. Carlson, and David S. Stephens. "Translocation and Surface Expression of Lipidated Serogroup B Capsular Polysaccharide in Neisseria meningitidis." Infection and Immunity 73, no. 3 (March 2005): 1491–505. http://dx.doi.org/10.1128/iai.73.3.1491-1505.2005.

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ABSTRACT The capsule of N. meningitidis serogroup B, (α2→8)-linked polysialic acid and the capsules of other meningococcal serogroups and of other gram-negative bacterial pathogens are anchored in the outer membrane through a 1,2-diacylglycerol moiety. Previous work on the meningococcal cps complex in Escherichia coli K-12 indicated that deletion of genes designated lipA and lipB caused intracellular accumulation of hyperelongated capsule polymers lacking the phospholipid substitution. To better understand the role of lip and lipB in capsule expression in a meningococcal background, the locati

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21

Маркелова, Н. Ю., and N. Yu Markelova. "REP-elements of the Escherichia coli Genome and Transcription Signals: Positional and Functional Analysis." Mathematical Biology and Bioinformatics 10, no. 1 (June 24, 2015): 245–59. http://dx.doi.org/10.17537/2015.10.245.

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In the intergenic regions of the Escherichia coli genome there are 356 REP- elements, containing 1-12 repeated sequences with degenerated consensus. Their biological role is poorly understood, but multiplicity in the genome, preferential localization between convergent genes and ability to form hairpin structures have led to the assumption that REP-elements participate in the transcription termination and processes affecting stability of the corresponding RNAs. Though the direct experiments did not confirm the ability of the model REP-sequence to stop RNA synthesis leaving some ambiguity regar

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22

Jürgen, Britta, Antje Breitenstein, Vlada Urlacher, Knut Büttner, Hongying Lin, Michael Hecker, Thomas Schweder, and Peter Neubauer. "Quality control of inclusion bodies in Escherichia coli." Microbial Cell Factories 9, no. 1 (2010): 41. http://dx.doi.org/10.1186/1475-2859-9-41.

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23

HARTLEY, D. L., and J. F. KANE. "Properties of inclusion bodies from recombinant Escherichia coli." Biochemical Society Transactions 16, no. 2 (April 1, 1988): 101–2. http://dx.doi.org/10.1042/bst0160101.

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24

Gilchuk, P. V. "Evaluation of renaturation methods for industrial obtaining of recombinant proteins from Escherichia coli inclusion bodies in biologically active form." Biopolymers and Cell 20, no. 3 (May 20, 2004): 182–92. http://dx.doi.org/10.7124/bc.0006a5.

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25

Simpson, R. J. "Solubilization of Escherichia coli Recombinant Proteins from Inclusion Bodies." Cold Spring Harbor Protocols 2010, no. 9 (September 1, 2010): pdb.prot5485. http://dx.doi.org/10.1101/pdb.prot5485.

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26

Kane, James F., and Donna L. Hartley. "Formation of recombinant protein inclusion bodies in Escherichia coli." Trends in Biotechnology 6, no. 5 (May 1988): 95–101. http://dx.doi.org/10.1016/0167-7799(88)90065-0.

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27

Upadhyay, Vaibhav, Anupam Singh, and Amulya K. Panda. "Purification of recombinant ovalbumin from inclusion bodies of Escherichia coli." Protein Expression and Purification 117 (January 2016): 52–58. http://dx.doi.org/10.1016/j.pep.2015.09.015.

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28

Bowden, Gregory A., Angel M. Paredes, and George Georgiou. "Structure and Morphology of Protein Inclusion Bodies in Escherichia Coli." Nature Biotechnology 9, no. 8 (August 1991): 725–30. http://dx.doi.org/10.1038/nbt0891-725.

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29

Rueda, Fabián, Olivia Cano-Garrido, Uwe Mamat, Kathleen Wilke, Joaquin Seras-Franzoso, Elena García-Fruitós, and Antonio Villaverde. "Production of functional inclusion bodies in endotoxin-free Escherichia coli." Applied Microbiology and Biotechnology 98, no. 22 (August 17, 2014): 9229–38. http://dx.doi.org/10.1007/s00253-014-6008-9.

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30

Carrió, M. Mar, and Antonio Villaverde. "Localization of Chaperones DnaK and GroEL in Bacterial Inclusion Bodies." Journal of Bacteriology 187, no. 10 (May 15, 2005): 3599–601. http://dx.doi.org/10.1128/jb.187.10.3599-3601.2005.

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ABSTRACT By immunostaining and transmission electron microscopy, chaperones DnaK and GroEL have been identified at the solvent-exposed surface of bacterial inclusion bodies and entrapped within these aggregates, respectively. Functional implications of this distinct localization are discussed in the context of Escherichia coli protein quality control.

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31

Allam, Ayman B., Leticia Reyes, Nacyra Assad-Garcia, John I. Glass, and Mary B. Brown. "Enhancement of Targeted Homologous Recombination in Mycoplasma mycoides subsp. capri by Inclusion of Heterologous recA." Applied and Environmental Microbiology 76, no. 20 (August 27, 2010): 6951–54. http://dx.doi.org/10.1128/aem.00056-10.

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ABSTRACT A suicide plasmid, pExp1-ctpA::tetM-recAec, employing recA from Escherichia coli and tetM as a selection marker, was used to generate ctpA knockout mutants in Mycoplasma mycoides subsp. capri through targeted gene disruption. Inclusion of E. coli recA greatly enhanced both the consistency and the recovery of mutants generated by homologous recombination.

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32

Hart, R. A., U. Rinas, and J. E. Bailey. "Protein composition of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli." Journal of Biological Chemistry 265, no. 21 (July 1990): 12728–33. http://dx.doi.org/10.1016/s0021-9258(19)38405-4.

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33

McCaman, M. T. "Fragments of prochymosin produced in Escherichia coli form insoluble inclusion bodies." Journal of Bacteriology 171, no. 2 (1989): 1225–27. http://dx.doi.org/10.1128/jb.171.2.1225-1227.1989.

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34

Carretas-Valdez, Manuel I., Francisco J. Cinco-Moroyoqui, Marina J. Ezquerra-Brauer, Enrique Marquez-Rios, Idania E. Quintero-Reyes, Alonso A. Lopez-Zavala, and Aldo A. Arvizu-Flores. "Refolding and Activation from Bacterial Inclusion Bodies of Trypsin I from Sardine (Sardinops sagax caerulea)." Protein & Peptide Letters 26, no. 3 (March 15, 2019): 170–75. http://dx.doi.org/10.2174/0929866525666181019161114.

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Background: Trypsin from fish species is considered as a cold-adapted enzyme that may find potential biotechnological applications. In this work, the recombinant expression, refolding and activation of Trypsin I (TryI) from Monterey sardine (Sardinops sagax caerulea) are reported. Methods: TryI was overexpressed in Escherichia coli BL21 as a fusion protein of trypsinogen with thioredoxin. Refolding of trypsinogen I was achieved by dialysis of bacterial inclusion bodies with a recovery of 16.32 mg per liter of Luria broth medium. Results: Before activation, the trypsinogen fusion protein did no

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35

Di Lorenzo, Mirella, Aurelio Hidalgo, Michael Haas, and Uwe T. Bornscheuer. "Heterologous Production of Functional Forms of Rhizopus oryzae Lipase in Escherichia coli." Applied and Environmental Microbiology 71, no. 12 (December 2005): 8974–77. http://dx.doi.org/10.1128/aem.71.12.8974-8977.2005.

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ABSTRACT To date, expression of the lipase from Rhizopus oryzae (ROL) in Escherichia coli always led to the formation of inclusion bodies and inactive protein. However, the production of active ROL and its precursor ProROL in soluble form was achieved when E. coli Origami(DE3) and pET-11d were used as expression systems.

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36

Lee, Sang-Eun. "Galactooligosaccharide Synthesis by Active β-Galactosidase Inclusion Bodies-Containing Escherichia coli Cells". Journal of Microbiology and Biotechnology 21, № 11 (28 листопада 2011): 1151–58. http://dx.doi.org/10.4014/jmb.1105.05021.

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37

Morreale, G. "Continuous processing of fusion protein expressed as an Escherichia coli inclusion body." Journal of Chromatography B 786, no. 1-2 (March 25, 2003): 237–46. http://dx.doi.org/10.1016/s1570-0232(02)00718-3.

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38

Lipničanová, Sabina, Daniela Chmelová, Andrej Godány, Miroslav Ondrejovič, and Stanislav Miertuš. "Purification of viral neuraminidase from inclusion bodies produced by recombinant Escherichia coli." Journal of Biotechnology 316 (June 2020): 27–34. http://dx.doi.org/10.1016/j.jbiotec.2020.04.005.

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39

Hwang, Soon Ook. "Effect of inclusion bodies on the buoyant density of recombinant Escherichia coli." Biotechnology Techniques 10, no. 3 (March 1996): 157–60. http://dx.doi.org/10.1007/bf00158938.

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40

Ni, He, Peng-Cheng Guo, Wei-Ling Jiang, Xiao-Min Fan, Xiang-Yu Luo, and Hai-Hang Li. "Expression of nattokinase in Escherichia coli and renaturation of its inclusion body." Journal of Biotechnology 231 (August 2016): 65–71. http://dx.doi.org/10.1016/j.jbiotec.2016.05.034.

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41

Xia, Xiao-Xia, Ya-Ling Shen, and Dong-Zhi Wei. "Purification and Characterization of Recombinant sTRAIL Expressed in Escherichia coli." Acta Biochimica et Biophysica Sinica 36, no. 2 (February 1, 2004): 118–22. http://dx.doi.org/10.1093/abbs/36.2.118.

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Abstract As a potential anti-tumor protein, tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) has drawn considerable attention. This report presented the purification and characterization of soluble TRAIL, expressed as inclusion bodies in E. coli. sTRAIL inclusion bodies were solubilized and refolded at a high concentration up to 0.9 g/L by a simple dilution method. Refolded protein was purified to electrophoretic homogeneity by a single-step immobilized metal affinity chromatography. The purified sTRAIL had a strong cytotoxic activity against human pancreatic tumor cell line 199

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42

Dolgikh, V. V., I. V. Senderskiy, G. V. Tetz, and V. V. Tetz. "Optimization of the Protocol for the Isolation and Refolding of the Extracellular Domain of HER2 Expressed in Escherichia coli." Acta Naturae 6, no. 2 (June 15, 2014): 106–9. http://dx.doi.org/10.32607/20758251-2014-6-2-106-109.

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Receptor 2 of the human epidermal growth factor (HER2/neu, c-erbB2) is a 185 kDa proto-oncogene protein characterized by an overexpression in some oncological diseases, including 30% of mammary glands cancers, as well as tumors in the ovary, stomach and other organs of the human body. Since HER2- tumor status testing is the essential part of a successful cancer treatment, the expression and purification of substantial amounts of the extracellular domain (ECD) of HER2 is an important task. The production of ECD HER2 in Escherichia coli has several advantages over the use of eukaryotic expressio

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43

Awofisayo-Okuyelu, Adedoyin, Julii Brainard, Ian Hall, and Noel McCarthy. "Incubation Period of Shiga Toxin–Producing Escherichia coli." Epidemiologic Reviews 41, no. 1 (2019): 121–29. http://dx.doi.org/10.1093/epirev/mxz001.

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Abstract Shiga toxin–producing Escherichia coli are pathogenic bacteria found in the gastrointestinal tract of humans. Severe infections could lead to life-threatening complications, especially in young children and the elderly. Understanding the distribution of the incubation period, which is currently inconsistent and ambiguous, can help in controlling the burden of disease. We conducted a systematic review of outbreak investigation reports, extracted individual incubation data and summary estimates, tested for heterogeneity, classified studies into subgroups with limited heterogeneity, and

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44

Alimuddin, Alimuddin, Indra Lesmana, Agus Oman Sudrajat, Odang Carman, and Irvan Faizal. "PRODUCTION AND BIOACTIVITY POTENTIAL OF THREE RECOMBINANT GROWTH HORMONES OF FARMED FISH." Indonesian Aquaculture Journal 5, no. 1 (June 30, 2010): 11. http://dx.doi.org/10.15578/iaj.5.1.2010.11-17.

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This study was aimed to produce recombinant growth hormone (rGH) from giant grouper (Epinephelus lanceolatus), giant gouramy (Osphronemus gouramy) and common carp (Cyprinus carpio) and compare their bioactivity potential by means of inducing the growth hormone of juvenile Nile tilapia (Oreochromis niloticus) as the model. DNA fragment encoding mature GH protein of giant grouper (El-mGH), giant gouramy (Og-mGH) and common carp (Cc-mGH) was amplified by PCR method. The purified PCR products were ligated to pCold-1 to generate pCold/El-mGH, pCold/OgmGH, and pCold/Cc-mGH protein expression vector,

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45

Fan, Gaofu, Zhiguo Yu, Jie Tang, Ruomeng Dai та Zhenguo Xu. "Preparation of gallic acid-hydroxypropyl-β-cyclodextrin inclusion compound and study on its effect mechanism on Escherichia coli in vitro". Materials Express 11, № 5 (1 травня 2021): 655–62. http://dx.doi.org/10.1166/mex.2021.1968.

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The purpose of this paper is to optimize the preparation process of gallic acid-hydroxypropyl-β-cyclodextrin inclusion compound and to study its antibacterial effect in vitro. Orthogonal test was used to screen the preparation method of the compound. The microscopic appearance of the compound was observed by microscope, and the solubility of the compound was detected by the dissolution method. The antibacterial activity of the compound was measured by the Oxford cup method. Under the transmission electron microscope, the microstructure of the cells and the intracellular ultrastructure changes

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46

McCusker, Emily, та Anne Skaja Robinson. "Refolding of G protein α subunits from inclusion bodies expressed in Escherichia coli". Protein Expression and Purification 58, № 2 (квітень 2008): 342–55. http://dx.doi.org/10.1016/j.pep.2007.11.015.

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47

Huang, Liurong, Haile Ma, Yunliang Li, and Shuxiang Li. "Antihypertensive activity of recombinant peptide IYPR expressed in Escherichia coli as inclusion bodies." Protein Expression and Purification 83, no. 1 (May 2012): 15–20. http://dx.doi.org/10.1016/j.pep.2012.02.004.

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48

Valax, Pascal, and George Georgiou. "Molecular characterization of .beta.-lactamase inclusion bodies produced in Escherichia coli. 1. Composition." Biotechnology Progress 9, no. 5 (September 1993): 539–47. http://dx.doi.org/10.1021/bp00023a014.

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Georgiou, G., J. N. Telford, M. L. Shuler, and D. B. Wilson. "Localization of inclusion bodies in Escherichia coli overproducing beta-lactamase or alkaline phosphatase." Applied and Environmental Microbiology 52, no. 5 (1986): 1157–61. http://dx.doi.org/10.1128/aem.52.5.1157-1161.1986.

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50

Sinacola, Jessica R., and Anne S. Robinson. "Rapid refolding and polishing of single-chain antibodies from Escherichia coli inclusion bodies." Protein Expression and Purification 26, no. 2 (November 2002): 301–8. http://dx.doi.org/10.1016/s1046-5928(02)00538-7.

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