Academic literature on the topic 'Salmonella typhimurium LT 2'
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Salmonella typhimurium LT 2.'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Journal articles on the topic "Salmonella typhimurium LT 2"
Fernández-Briera, Almudena, and Amando Garrido-Pertierra. "A degradation pathway of propionate in Salmonella typhimurium LT-2." Biochimie 70, no. 6 (June 1988): 757–68. http://dx.doi.org/10.1016/0300-9084(88)90105-8.
Full textŠišák, F., H. Havlíčková, R. Karpíšková, and I. Rychlík. "Prevalence of Salmonellae and their resistance to antibiotics in slaughtered pigs in the Czech Republic." Czech Journal of Food Sciences 22, No. 6 (November 16, 2011): 230–36. http://dx.doi.org/10.17221/3428-cjfs.
Full textJUNG, YONG SOO, ROBIN C. ANDERSON, JAMES A. BYRD, THOMAS S. EDRINGTON, RANDLE W. MOORE, TODD R. CALLAWAY, JACK McREYNOLDS, and DAVID J. NISBET. "Reduction of Salmonella Typhimurium in Experimentally Challenged Broilers by Nitrate Adaptation and Chlorate Supplementation in Drinking Water†." Journal of Food Protection 66, no. 4 (April 1, 2003): 660–63. http://dx.doi.org/10.4315/0362-028x-66.4.660.
Full textBarrell, R. A. E. "Isolations of salmonellas from humans and foods in the Manchester area: 1981–1985." Epidemiology and Infection 98, no. 3 (June 1987): 277–84. http://dx.doi.org/10.1017/s0950268800062038.
Full textAbdelhadi, Iman M. A., Ahmed R. Sofy, Ahmed A. Hmed, Ehab E. Refaey, Hany E. Soweha, and Mohamed A. Abbas. "Discovery of Polyvalent Myovirus (vB_STM-2) Phage as a Natural Antimicrobial System to Lysis and Biofilm Removal of Salmonella Typhimurium Isolates from Various Food Sources." Sustainability 13, no. 21 (October 20, 2021): 11602. http://dx.doi.org/10.3390/su132111602.
Full textSAWYER, J. E., S. T. GREINER, G. R. ACUFF, L. M. LUCIA, E. CABRERA-DIAZ, and D. S. HALE. "Effect of Xylitol on Adhesion of Salmonella Typhimurium and Escherichia coli O157:H7 to Beef Carcass Surfaces." Journal of Food Protection 71, no. 2 (February 1, 2008): 405–10. http://dx.doi.org/10.4315/0362-028x-71.2.405.
Full textCOCHRANE, ROGER A., ANNE R. HUSS, GREGORY C. ALDRICH, CHARLES R. STARK, and CASSANDRA K. JONES. "Evaluating Chemical Mitigation of Salmonella Typhimurium ATCC 14028 in Animal Feed Ingredients." Journal of Food Protection 79, no. 4 (April 1, 2016): 672–76. http://dx.doi.org/10.4315/0362-028x.jfp-15-320.
Full textJUNG, YONG SOO, ROBIN C. ANDERSON, THOMAS S. EDRINGTON, KENNETH J. GENOVESE, J. ALLEN BYRD, TODD R. CALLAWAY, and DAVID J. NISBET. "Experimental Use of 2-Nitropropanol for Reduction of Salmonella Typhimurium in the Ceca of Broiler Chicks†‡." Journal of Food Protection 67, no. 9 (September 1, 2004): 1945–47. http://dx.doi.org/10.4315/0362-028x-67.9.1945.
Full textSantana, Eliete Souza, Maria Auxiliadora Andrade, Marcos Barcelos Café, José Henrique Stringhini, Tatiane Martins Rocha, and Valéria de Sá Jaime. "Efeitos da lactulose na saúde gastrointestinal de frangos de corte experimentalmente inoculados com Salmonella entérica sorovar Typhimurium." Ciência Animal Brasileira 15, no. 2 (June 2014): 187–94. http://dx.doi.org/10.1590/1809-6891v15i13604.
Full textSaw, Seow Hoon, J. L. Mak, M. H. Tan, S. T. Teo, T. Y. Tan, M. Y. K. Cheow, C. A. Ong, et al. "Detection and quantification of Salmonella in fresh vegetables in Perak, Malaysia." Food Research 4, no. 2 (October 27, 2019): 441–48. http://dx.doi.org/10.26656/fr.2017.4(2).316.
Full textDissertations / Theses on the topic "Salmonella typhimurium LT 2"
Simmons, James Walter. "O-Acetylserine Sulhydralase-A from Salmonella typhimurium LT-2: Thermodynamic Properties and SPectral Identification of Intermediates." Thesis, University of North Texas, 1993. https://digital.library.unt.edu/ark:/67531/metadc278042/.
Full textŽindul, Adam. "Salmonella enterica Serovar Typhimurium inaktyvacijos fotosensibilizacija vertinimas ir poveikio modeliavimas." Master's thesis, Lithuanian Academic Libraries Network (LABT), 2014. http://vddb.library.lt/obj/LT-eLABa-0001:E.02~2011~D_20140701_164247-99768.
Full textEvaluation of Salmonella enterica Serovar Typhimurium inactivation by photosensitization and impact modeling The aim goal of this research is to evaluate the influence of irradiation of UV light and incubation period on Salmonella enterica Serovar Typhimurium bacteria. Shortly discussed most commonly used mathematical models of bacterial inactivation, expressed lag phase and its function. Next step is evaluation of line part and tail of inactivation (mortality) curve. At the end of the research the inactivation formula is deduced and the results are discussed.
Figueira, Ana Rita. "Analysis of effectors of the Salmonella Typhimurium SPI-2 type three secretion system." Thesis, Imperial College London, 2011. http://hdl.handle.net/10044/1/9287.
Full textKrogan, Nevan John. "Utilization of dihydroorotate by S. typhimurium LT-2, characterization of the dhpA gene." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0007/MQ45331.pdf.
Full textCea, Medina Pablo Antonio. "Caracterización bioquímica de la 4-amino-5-hidroximetil-2-metilpirimidina quinasa de Salmonella typhimurium y Thermus thermophilus." Tesis, Universidad de Chile, 2019. http://repositorio.uchile.cl/handle/2250/168116.
Full textLa 4-amino-5-hidroximetil-2-metilpirimidina quinasa (HMPK, EC 2.7.1.49) es una enzima perteneciente a la superfamilia riboquinasa y participa en la biosíntesis de tiamina (vitamina B1) en bacterias. Se ha descrito que esta enzima es capaz de catalizar dos fosforilaciones consecutivas dependientes de ATP altamente específicas sobre el sustrato hidroximetil pirimidina (HMP), generando como producto hidroximetil pirimidina pirofosfato. Esto contrasta notablemente con lo que se ha observado en las piridoxal quinasas de bacterias Gram positivas (HMPK/PLK, EC 2.7.1.35), un grupo de enzimas homólogas cercanas capaces de fosforilar hidroximetil pirimidina, piridoxal, piridoxina y piridoxamina, pero incapaces de catalizar dos fosforilaciones consecutivas, por lo que sólo producen hidroximetil pirimidina fosfato. Las HMPKs no han sido estudiadas tan exhaustivamente como las HMPK/PLKs y sólo hay dos caracterizaciones breves disponibles en la literatura; la de la HMPK de Escherichia coli y la de Bacillus subtilis. Por lo tanto, aún no se conoce si las propiedades observadas en las enzimas descritas son ubicuas para linajes bacterianos distintos, especialmente aquellos filogenéticamente distantes y que han sido sometido a presiones selectivas fuertes, como los extremófilos. Por esta razón, en este trabajo se realizó la caracterización bioquímica de la HMPK de la enterobacteria Salmonella typhimurium (StHMPK) y de la bacteria termófila Thermus thermophilus (TtHMPK). A través de experimentos de estequiometría de reacción y análisis de generación de productos, se demostró que ambas enzimas son capaces de catalizar dos fosforilaciones consecutivas. Experimentos de especificidad de sustrato revelaron que ambas enzimas son altamente específicas por hidroximetil pirimidina. Análisis filogenéticos mostraron que estas enzimas están estrechamente relacionadas con las HMPKs/PLK de organismos gram positivos, y estas últimas parecen ser descendientes directos de las HMPKs. Por lo tanto, para estudiar cómo estos grupos de enzimas han divergido en términos de sus actividades catalíticas, se realizaron simulaciones de dinámica molecular del complejo ternario (Mg·ATP - HMP) de StHMPK, para analizar el sitio de unión a sustrato y compararlo con el de la HMPK/PLK de Staphylococcus aureus (SaPLK). Los resultados mostraron que existe un alto grado de conservación entre ambos sitios, existiendo sólo unas pocas diferencias que podrían explicar la divergencia funcional observada, principalmente la presencia de una treonina adyacente a la base catalítica en StHMPK, que es reemplazada por una alanina en SaPLK, y la presencia de una glutamina en StHMPK que forma puentes de hidrógeno con el HMP. La caracterización cinética de StHMPK y TtHMPK mostró que ambas enzimas poseen una KM similar para HMP (cercana a 30μM) y que la Vmax para TtHMPK es un orden de magnitud menor que para StHMPK a 37 °C. Sin embargo, estos parámetros fueron obtenidos para las curvas de saturación de HMP, las cuales mostraban un comportamiento del tipo Michaelis-Menten, mientras que las curvas de saturación para ATP mostraron una clara desviación de este modelo y por lo tanto, no se pudieron determinar parámetros cinéticos. Finalmente, se realizó una caracterización estructural y biofísica para evaluar diferencias de estabilidad. Ambas enzimas parecen ser monómeros en las condiciones estudiadas, a diferencia de lo reportado para la enzima de E. coli que forma un tetrámero. Experimentos de desplegamiento por temperatura y agentes químicos mostraron que TtHMPK es significativamente más estable que StHMPK. Las bases estructurales de estas diferencias fueron analizadas mediante simulaciones de dinámica molecular, las que revelaron que la proteína termoestable es más rígida, tiene un menor contenido de residuos polares en el núcleo y tiene mayor cantidad de interacciones electrostáticas que su homólogo mesoestable.
4-amino-5-hydroxymethyl-2-methylpyrimidine kinase (HMPK, EC 2.7.1.49) is a bacterial enzyme that belongs to the ribokinase superfamily and participates in the thiamine (vitamine B1) biosynthetic pathway. It has been described that this enzyme is capable to catalyze two consecutive highly specific ATP dependent phosphorylations on the substrate hydroxymethyl pyrimidine, yielding hydroxymethyl pyrimidine pyrophosphate. This contrast notoriously with what has been observed for the closely related homologous enzymes pyridoxal kinases from Gram positive bacteria (HMPK/PLK, EC 2.7.1.35), which can phosphorylate hydroxymethyl pyrimidine, pyridoxal, pyridoxine and pyridoxamine, but are unable to catalyze two consecutive phosphorylations, thus only produce hydroxymethyl pyrimidine phosphate. HMPKs have not been as extensively studied as HMPKs/PLK, and only two brief biochemical characterizations are available on the literature; the characterization of the HMPK from Escherichia coli and from Bacillus subtilis. Therefore, it is still unknown whether the properties observed in the described enzymes are ubiquitous among different bacterial lineages, especially those that come from a very distinct phylogenetic background and have been subject to strong selective pressures, as the enzymes from extremophilic organisms. For this reason, in this work we address the biochemical characterization of the HMPK from the enterobacteria Salmonella typhimurium (StHMPK) and the thermophilic bacteria Thermus thermophilus (TtHMPK). Through stoichiometric experiments and product generation analysis, it was established that both enzymes are able to perform two consecutive phosphorylations. Substrate specificity experiments revealed that both enzymes are highly specific for hydroxymethyl pyrimidine. Phylogenetic analysis of these enzymes showed that are closely related to HMPKs/PLK from Gram positive organisms, being the later a direct descendant from HMPKs. Therefore, to study how these two groups of enzymes have diverged so much in terms of their catalytic activities, we analysed the substrate binding site of StHMPK by molecular dynamics simulations of the ternary complex (Mg·ATP - HMP) and compared it to the binding site of the PLK from Staphylococcus aureus (SaPLK). The results showed that there is an overall great conservation among the active sites, with just a few differences that could be responsible for the functional divergences observed, mainly the presence of a threonine residue adjacent to the catalytic base in StHMPK which is replaced by an alanine in SaPLK, and the presence of a glutamine that forms hydrogen bonds with the HMP in StHMPK. Kinetic characterization of StHMPK and TtHMPK showed that both enzymes have a similar KM for HMP (around 30 μM) while the Vmax for TtHMPK is one order of magnitude lower than the Vmax for StHMPK. However, these parameters were obtained only for HMP saturation curves, which showed a Michaelis-Menten behaviour, whereas ATP saturation curves displayed a clear deviation from a Michaelis-Menten model and therefore, no kinetic parameters could be deduced from these experiments. Finally, a biophysical and structural characterization to assess stability differences was performed. Both enzymes seem to be in monomeric state under the conditions assayed, in contrast with what was reported for the enzyme from E. coli, which forms a tetramer. Thermal and chemical unfolding experiments showed that TtHMPK is significantly more stable than StHMPK. The structural basis for these differences were investigated through molecular dynamics simulations, which revealed that the thermostable protein is more rigid, has a reduced content of polar amino acids in its core, and has more electrostatic interactions than its mesostable homologous.
Julio del 2019
Barreto, Arce Liz Judith. "Efecto de la lactoferrina bovina en la invasión de Salmonella typhimurium cepa SL 1344 a células HEp-2." Master's thesis, Universidad Nacional Mayor de San Marcos, 2017. https://hdl.handle.net/20.500.12672/6131.
Full textTesis
Havemann, Gregory Dale. "Polyhedral Organelles involved in the B12-dependent metabolism of 1, 2-propanediol in Salmonella enterica serovar typhimurium LT2." [Gainesville, Fla.] : University of Florida, 2003. http://purl.fcla.edu/fcla/etd/UFE0000697.
Full textMarjoshi, Delphine. "Investigating the effects of three herbicides - Kamba, 2,4-D and Roundup on Salmonella enteric serovar Typhimurium growth and antibiotic tolerance phenotypes." Thesis, University of Canterbury. School of Biological Sciences, 2014. http://hdl.handle.net/10092/10284.
Full textRaux, Evelyne Christine. "Biosynthesis of cobalamin (vitamin Bâ†1â†2) in Salmonella typhimurium and Bacillus megaterium de Bary : characterisation of the anaerobic pathway." Thesis, University College London (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.313359.
Full textDeschenes, Marianne. "Régulation de la réponse immunitaire in vivo et in vitro au cours de l'infection chronique par Salmonella typhimurium." Paris 11, 1989. http://www.theses.fr/1989PA114803.
Full textBooks on the topic "Salmonella typhimurium LT 2"
(Editor), Frederick C. Neidhardt, and Roy Curtiss (Editor), eds. Escherichia Coli and Salmonella (2 Volume Set: Cellular and Molecular Biology. 2nd ed. ASM Press, 1996.
Find full textBook chapters on the topic "Salmonella typhimurium LT 2"
Isaacson, R. E., C. Argyilan, L. Kwan, S. Patterson, and K. Yoshinaga. "Phase Variable Switching of in Vivo and Environmental Phenotypes of Salmonella Typhimurium." In Mechanisms in the Pathogenesis of Enteric Diseases 2, 281–89. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4143-1_30.
Full textMehta, Alka, Surjit Singh, and Nirmal Kumar Ganguly. "Effect of Salmonella typhimurium enterotoxin (S-LT) on lipid peroxidation and cell viability levels of isolated rat enterocytes." In Stress Adaptation, Prophylaxis and Treatment, 175–81. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-5097-6_22.
Full textSternberg, Nat L., and Russell Maurer. "[2] Bacteriophage-mediated generalized transduction in Escherichia coli and Salmonella typhimurium." In Methods in Enzymology, 18–43. Elsevier, 1991. http://dx.doi.org/10.1016/0076-6879(91)04004-8.
Full textTsuruda, Carina Terumi, Patrícia Canteri De Souza, Erick Kenji Nishio, Ricardo Sérgio Couto de Almeida, Luciano Aparecido Panagio, Ana Angelita Sampaio Baptista, Sandra Garcia, Renata Katsuko Takayama Kobayashi, and Gerson Nakazato. "AVALIAÇÃO DO EFEITO PROBIÓTICO DE Lactobacillus rhamnosus V5 CONTRA SALMONELLA ENTERICA sorovariedade Typhimurium." In Análise Crítica das Ciências Biológicas e da Natureza 2, 231–40. Atena Editora, 2019. http://dx.doi.org/10.22533/at.ed.58319270521.
Full textZamri, Amir Izzwan, Nor Hazwani Mohd Hasali, Muhammad Hariz Mohd Hasali, Tuan Zainazor Tuan Chilek, Fisal Ahmad, and Mohd Khairi Mohamed Zainol. "Microbiological Diversity and Properties of Stingless Bee Honey." In Advances in Environmental Engineering and Green Technologies, 141–52. IGI Global, 2023. http://dx.doi.org/10.4018/978-1-6684-6265-2.ch008.
Full textMedeiros, A. R. S., M. V. S. Couto, T. Z. Rodrigues, J. G. Santos, E. F. Garcia, and P. P. F. Vieira. "APLICAÇÃO DE CRISTALIZAÇÃO EM FRUTAS EM DIFERENTES ESTAGIOS DE MATURAÇÃO E SUA QUALIDADE." In Ciência e Tecnologia de Alimentos: Pesquisas e Avanços. Agron Food Academy, 2022. http://dx.doi.org/10.53934/9786599539664-41.
Full textConference papers on the topic "Salmonella typhimurium LT 2"
Wen, Tao, Ronghui Wang, America F. Sotero, and Yanbin Li. "A Portable Impedance Immunosensing System for Rapid Detection of <i>Salmonella</i> Typhimurium." In 2017 Spokane, Washington July 16 - July 19, 2017. St. Joseph, MI: American Society of Agricultural and Biological Engineers, 2017. http://dx.doi.org/10.13031/aim.201700368.
Full textSotero, America F., Ronghui Wang, Wen Tao, Benhua Zhang, and Yanbin Li. "<i>A Portable Impedance Aptasensing System for Rapid Detection of Salmonella Typhimurium in Poultry Products</i>." In 2018 Detroit, Michigan July 29 - August 1, 2018. St. Joseph, MI: American Society of Agricultural and Biological Engineers, 2018. http://dx.doi.org/10.13031/aim.201801147.
Full textHaesebrouck, Freddy, F. Boyen, J. Volf, N. Botteldoorn, C. Adriaensen, J. P. Hernalsteens, R. Ducatelle, F. van Immerseel, M. Heyndrickx, and F. Pasmans. "SPI-2 of Salmonella Typhimurium is not necessary for long term colonization of pigs." In Seventh International Symposium on the Epidemiology and Control of Foodborne Pathogens in Pork. Iowa State University, Digital Press, 2007. http://dx.doi.org/10.31274/safepork-180809-112.
Full textHorikawa, Shin, Kiril A. Vaglenov, Dana M. Gerken, Yating Chai, Mi-Kyung Park, Suiqiong Li, Valery A. Petrenko, and Bryan A. Chin. "Rapid, enhanced detection of <i>Salmonella Typhimurium</i> on fresh spinach leaves using micron-scale, phage-coated magnetoelastic biosensors." In SPIE Defense, Security, and Sensing. SPIE, 2012. http://dx.doi.org/10.1117/12.920456.
Full textCappuyns, Astrid M., Kristel Bernaerts, Sigrid C. De Keersmaecker, and Jan F. Van Impe. "A simple structured model for growth and AI-2 mediated cell-cell communication of Salmonella Typhimurium." In Automation (MED 2008). IEEE, 2008. http://dx.doi.org/10.1109/med.2008.4602087.
Full textAugustine, Shancy, Pan Gu, Xiangjun Zheng, Toshikazu Nishida, and Z. Hugh Fan. "Development of All-Plastic Microvalve Array for Multiplexed Immunoassay." In ASME 2014 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2014. http://dx.doi.org/10.1115/imece2014-38154.
Full textReports on the topic "Salmonella typhimurium LT 2"
Irudayaraj, Joseph, Ze'ev Schmilovitch, Amos Mizrach, Giora Kritzman, and Chitrita DebRoy. Rapid detection of food borne pathogens and non-pathogens in fresh produce using FT-IRS and raman spectroscopy. United States Department of Agriculture, October 2004. http://dx.doi.org/10.32747/2004.7587221.bard.
Full textSchat, Karel Antoni, Irit Davidson, and Dan Heller. Chicken infectious anemia virus: immunosuppression, transmission and impact on other diseases. United States Department of Agriculture, 2008. http://dx.doi.org/10.32747/2008.7695591.bard.
Full textWillis, C., F. Jorgensen, S. A. Cawthraw, H. Aird, S. Lai, M. Chattaway, I. Lock, E. Quill, and G. Raykova. A survey of Salmonella, Escherichia coli (E. coli) and antimicrobial resistance in frozen, part-cooked, breaded or battered poultry products on retail sale in the United Kingdom. Food Standards Agency, May 2022. http://dx.doi.org/10.46756/sci.fsa.xvu389.
Full text