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Auswahl der wissenschaftlichen Literatur zum Thema „Selenomonas ruminantium“
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Zeitschriftenartikel zum Thema "Selenomonas ruminantium"
Michel, Tomas A., und Joan M. Macy. „Ferredoxin from Selenomonas ruminantium“. Archives of Microbiology 153, Nr. 5 (April 1990): 518–20. http://dx.doi.org/10.1007/bf00248437.
Der volle Inhalt der QuelleKalmokoff, M. L., J. W. Austin, M. F. Whitford und R. M. Teather. „Characterization of a major envelope protein from the rumen anaerobeSelenomonas ruminantiumOB268“. Canadian Journal of Microbiology 46, Nr. 4 (01.04.2000): 295–303. http://dx.doi.org/10.1139/w99-149.
Der volle Inhalt der QuellePristas, Peter, und Maria Piknova. „Underrepresentation of short palindromes in Selenomonas ruminantium DNA: evidence for horizontal gene transfer of restriction and modification systems?“ Canadian Journal of Microbiology 51, Nr. 4 (01.04.2005): 315–18. http://dx.doi.org/10.1139/w05-004.
Der volle Inhalt der QuelleWiryawan, KG, und JD Brooker. „Probiotic control of lactate accumulation in acutely grain-fed sheep“. Australian Journal of Agricultural Research 46, Nr. 8 (1995): 1555. http://dx.doi.org/10.1071/ar9951555.
Der volle Inhalt der QuelleHaya, Shohei, Yuya Tokumaru, Naoki Abe, Jun Kaneko und Shin-ichi Aizawa. „Characterization of Lateral Flagella of Selenomonas ruminantium“. Applied and Environmental Microbiology 77, Nr. 8 (18.02.2011): 2799–802. http://dx.doi.org/10.1128/aem.00286-11.
Der volle Inhalt der QuelleFecskeová, Lívia, Peter Pristaš und Peter Javorský. „Cloning and characterization of cobA, one of vitamin B12 biosynthesis pathway genes from Selenomonas ruminantium“. Nova Biotechnologica et Chimica 10, Nr. 2 (31.08.2021): 131–35. http://dx.doi.org/10.36547/nbc.1122.
Der volle Inhalt der QuelleNisbet, David J., und Scott A. Martin. „Factors affecting L-lactate utilization by Selenomonas ruminantium“. Journal of Animal Science 72, Nr. 5 (01.05.1994): 1355–61. http://dx.doi.org/10.2527/1994.7251355x.
Der volle Inhalt der QuelleWilliams, D. K., und S. A. Martin. „Xylose uptake by the ruminal bacterium Selenomonas ruminantium.“ Applied and Environmental Microbiology 56, Nr. 6 (1990): 1683–88. http://dx.doi.org/10.1128/aem.56.6.1683-1688.1990.
Der volle Inhalt der QuelleBrooker, J. D., und B. Stokes. „Monoclonal antibodies against the ruminal bacterium Selenomonas ruminantium.“ Applied and Environmental Microbiology 56, Nr. 7 (1990): 2193–99. http://dx.doi.org/10.1128/aem.56.7.2193-2199.1990.
Der volle Inhalt der QuelleKopecny, J., V. Kostyukovsky und K. Fliegerova. „Electroporation of G+ host plasmids into Selenomonas ruminantium“. CrossRef Listing Of Deleted DOIs 45, Suppl. 1 (1996): 356. http://dx.doi.org/10.1051/rnd:19960685.
Der volle Inhalt der QuelleDissertationen zum Thema "Selenomonas ruminantium"
Cheong, Judy Poh Eng. „Characterisation of a temperate bacteriophage of the ruminal bacterium Selenomonas ruminantium“. Title page, contents and summary only, 1997. http://web4.library.adelaide.edu.au/theses/09PH/09phc5185.pdf.
Der volle Inhalt der QuelleGilmour, Martin. „Lactate utilisation in the rumen bacterium Selenomonas ruminantium“. Thesis, Heriot-Watt University, 1994. http://hdl.handle.net/10399/1379.
Der volle Inhalt der QuelleZhang, Ning. „Molecular characterization of the ruminal bacterial species Selenomonas ruminantium : a thesis submitted to the University of Adelaide for the degree of Doctor of Philosophy /“. Title page, contents and abstract only, 1992. http://web4.library.adelaide.edu.au/theses/09PH/09phn714.pdf.
Der volle Inhalt der QuelleIncludes two of author's articles in pocket inside back cover. Includes bibliographical references (leaves 133-150).
Robertson, J. D. „The energetics of end product excretion from a rumen bacterium, Selenomonas ruminantium“. Thesis, University of Aberdeen, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.373190.
Der volle Inhalt der QuelleRicke, Steven Clarence. „Characterization of hen egg yolk antibodies made to Selenomonas ruminantium, and growth and metabolic response of Selenomonas ruminantium HD₄ in high concentrations of ammonia“. 1989. http://catalog.hathitrust.org/api/volumes/oclc/22269780.html.
Der volle Inhalt der QuelleTypescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.
Zhang, Ning 1965. „Molecular characterization of the ruminal bacterial species Selenomonas ruminantium : a thesis submitted to the University of Adelaide for the degree of Doctor of Philosophy“. 1992. http://web4.library.adelaide.edu.au/theses/09PH/09phn714.pdf.
Der volle Inhalt der QuelleZhang, Ning 1965. „Molecular characterization of the ruminal bacterial species Selenomonas ruminantium / by Zhang Ning“. Thesis, 1992. http://hdl.handle.net/2440/21665.
Der volle Inhalt der QuelleIncludes bibliographical references (leaves 133-150)
xii, 150 leaves : ill. ; 30 cm.
Diversity in the ruminal Gram negative bacterial species Selenomonas ruminantium has been investigated by DNA fingerprinting, DNA homology and plasmid profile analysis. Twenty different isolates from the sheep rumen were classified morphologically and by carbon source utilization.
Thesis (Ph.D.)--University of Adelaide, Dept. of Animal Science, Waite Agricultural Research Institute, 1993
Hsu, ChingYi, und 許精益. „Analyzing the Active Site of Selenomonas ruminantium Phytase by Site-directed Mutagenesis and X-ray Crystallography“. Thesis, 2004. http://ndltd.ncl.edu.tw/handle/51404419758848221883.
Der volle Inhalt der Quelle國立臺灣大學
生化科學研究所
92
Phytase can hydrolyzes phytate（myo-inositol hexaphosphate）during plant germination to produce phosphate（Pi）and inositol polyphasphate derivatives. In poultry and pig farms, phytase and phytate are fed to livestock as additives to provide Pi. In this study, we analyzed the active site of Selenomous ruminantium phytase . It exhibits higher catalytic activity than many other phytases. We wish our analysis could improve its applicability in the livestock industry. Most phytases can be classified into two big families: Histidine acid phytase family and Alkaline phytase family. S. ruminantium phytase, however, belongs to neither of them. Through structural alignment we have found that the active site of S. ruminantium phytase greatly resembles to members of the dual specificity phosphatase family in that it contains conserved Cys241 in the primary catalytic site, P-loop, and Asp212 and Pro216 in the auxiliary site, WPD-loop. To study the functions of these conserved amino acid residues, we employed site-directed mutagenesis to change Cys241 into Ser241 or Ala241, and Asp212 and Pro216 into Ala212 and Gly216, respectively, and measured their catalytic activity of these mutant forms. We found that the activity of P216G decreases as the temperatures increases, whereas mutations in Cys241 and Asp212 abrogate the activity of S. ruminantium phytase. These results suggest that these sites are very important for the function of S. ruminantium phytase. We also examined CD spectra of these mutant forms to test whether the increase in temperature causes conformational changes. To better understand the structural properties of phytase and its interaction with the substrates, C241A recombinant protein is over expressed in E. coli, and crystallized by using sodium malonate as precipitant, and subject to X-ray crystallography. We found that malonate binds into the active site of C214A. This observation has gain insight that how the competitive inhibition of polycarboxyl acid acts to the phytase active site.
Hsu, Ching-Yi, und 許精益. „Analyzing the Active Site of Selenomonas ruminantium Phytase by Site-directed Mutagenesis and X-ray Crystallography“. Thesis, 2004. http://ndltd.ncl.edu.tw/handle/56405004965771563781.
Der volle Inhalt der Quelle國立臺灣大學
生化科學研究所
92
Phytase can hydrolyzes phytate（myo-inositol hexaphosphate）during plant germination to produce phosphate（Pi）and inositol polyphasphate derivatives. In poultry and pig farms, phytase and phytate are fed to livestock as additives to provide Pi. In this study, we analyzed the active site of Selenomous ruminantium phytase . It exhibits higher catalytic activity than many other phytases. We wish our analysis could improve its applicability in the livestock industry. Most phytases can be classified into two big families: Histidine acid phytase family and Alkaline phytase family. S. ruminantium phytase, however, belongs to neither of them. Through structural alignment we have found that the active site of S. ruminantium phytase greatly resembles to members of the dual specificity phosphatase family in that it contains conserved Cys241 in the primary catalytic site, P-loop, and Asp212 and Pro216 in the auxiliary site, WPD-loop. To study the functions of these conserved amino acid residues, we employed site-directed mutagenesis to change Cys241 into Ser241 or Ala241, and Asp212 and Pro216 into Ala212 and Gly216, respectively, and measured their catalytic activity of these mutant forms. We found that the activity of P216G decreases as the temperatures increases, whereas mutations in Cys241 and Asp212 abrogate the activity of S. ruminantium phytase. These results suggest that these sites are very important for the function of S. ruminantium phytase. We also examined CD spectra of these mutant forms to test whether the increase in temperature causes conformational changes. To better understand the structural properties of phytase and its interaction with the substrates, C241A recombinant protein is over expressed in E. coli, and crystallized by using sodium malonate as precipitant, and subject to X-ray crystallography. We found that malonate binds into the active site of C214A. This observation has gain insight that how the competitive inhibition of polycarboxyl acid acts to the phytase active site.
Buchteile zum Thema "Selenomonas ruminantium"
Jordan, Douglas B., Xin-Liang Li, Christopher A. Dunlap, Terence R. Whitehead und Michael A. Cotta. „β-d-Xylosidase From Selenomonas ruminantium of Glycoside Hydrolase Family 43“. In Applied Biochemistry and Biotecnology, 93–104. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-60327-181-3_9.
Der volle Inhalt der QuelleRichardson, Anthony J., und Colin S. Stewart. „Hydrogen Transfer Between Neocallimastix Frontalis and Selenomonas Ruminantium Grown in Mixed Culture“. In Microbiology and Biochemistry of Strict Anaerobes Involved in Interspecies Hydrogen Transfer, 463–65. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4613-0613-9_60.
Der volle Inhalt der QuelleJordan, Douglas B. „B-d-Xylosidase from Selenomonas ruminantium: Catalyzed Reactions with Natural and Artificial Substrates“. In Biotechnology for Fuels and Chemicals, 257–69. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-60327-526-2_27.
Der volle Inhalt der QuelleAizawa, Shin-Ichi. „Selenomonas ruminantium — The Authentic Lateral Flagella“. In The Flagellar World, 78–79. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-417234-0.00025-6.
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