Littérature scientifique sur le sujet « Selenomonas ruminantium »
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Articles de revues sur le sujet "Selenomonas ruminantium"
Michel, Tomas A., et Joan M. Macy. « Ferredoxin from Selenomonas ruminantium ». Archives of Microbiology 153, no 5 (avril 1990) : 518–20. http://dx.doi.org/10.1007/bf00248437.
Texte intégralKalmokoff, M. L., J. W. Austin, M. F. Whitford et R. M. Teather. « Characterization of a major envelope protein from the rumen anaerobeSelenomonas ruminantiumOB268 ». Canadian Journal of Microbiology 46, no 4 (1 avril 2000) : 295–303. http://dx.doi.org/10.1139/w99-149.
Texte intégralPristas, Peter, et 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, no 4 (1 avril 2005) : 315–18. http://dx.doi.org/10.1139/w05-004.
Texte intégralWiryawan, KG, et JD Brooker. « Probiotic control of lactate accumulation in acutely grain-fed sheep ». Australian Journal of Agricultural Research 46, no 8 (1995) : 1555. http://dx.doi.org/10.1071/ar9951555.
Texte intégralHaya, Shohei, Yuya Tokumaru, Naoki Abe, Jun Kaneko et Shin-ichi Aizawa. « Characterization of Lateral Flagella of Selenomonas ruminantium ». Applied and Environmental Microbiology 77, no 8 (18 février 2011) : 2799–802. http://dx.doi.org/10.1128/aem.00286-11.
Texte intégralFecskeová, Lívia, Peter Pristaš et Peter Javorský. « Cloning and characterization of cobA, one of vitamin B12 biosynthesis pathway genes from Selenomonas ruminantium ». Nova Biotechnologica et Chimica 10, no 2 (31 août 2021) : 131–35. http://dx.doi.org/10.36547/nbc.1122.
Texte intégralNisbet, David J., et Scott A. Martin. « Factors affecting L-lactate utilization by Selenomonas ruminantium ». Journal of Animal Science 72, no 5 (1 mai 1994) : 1355–61. http://dx.doi.org/10.2527/1994.7251355x.
Texte intégralWilliams, D. K., et S. A. Martin. « Xylose uptake by the ruminal bacterium Selenomonas ruminantium. » Applied and Environmental Microbiology 56, no 6 (1990) : 1683–88. http://dx.doi.org/10.1128/aem.56.6.1683-1688.1990.
Texte intégralBrooker, J. D., et B. Stokes. « Monoclonal antibodies against the ruminal bacterium Selenomonas ruminantium. » Applied and Environmental Microbiology 56, no 7 (1990) : 2193–99. http://dx.doi.org/10.1128/aem.56.7.2193-2199.1990.
Texte intégralKopecny, J., V. Kostyukovsky et 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.
Texte intégralThèses sur le sujet "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.
Texte intégralGilmour, Martin. « Lactate utilisation in the rumen bacterium Selenomonas ruminantium ». Thesis, Heriot-Watt University, 1994. http://hdl.handle.net/10399/1379.
Texte intégralZhang, 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.
Texte intégralIncludes 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.
Texte intégralRicke, 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.
Texte intégralTypescript. 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.
Texte intégralZhang, Ning 1965. « Molecular characterization of the ruminal bacterial species Selenomonas ruminantium / by Zhang Ning ». Thesis, 1992. http://hdl.handle.net/2440/21665.
Texte intégralIncludes 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, et 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.
Texte intégral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, et 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.
Texte intégral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.
Chapitres de livres sur le sujet "Selenomonas ruminantium"
Jordan, Douglas B., Xin-Liang Li, Christopher A. Dunlap, Terence R. Whitehead et Michael A. Cotta. « β-d-Xylosidase From Selenomonas ruminantium of Glycoside Hydrolase Family 43 ». Dans Applied Biochemistry and Biotecnology, 93–104. Totowa, NJ : Humana Press, 2007. http://dx.doi.org/10.1007/978-1-60327-181-3_9.
Texte intégralRichardson, Anthony J., et Colin S. Stewart. « Hydrogen Transfer Between Neocallimastix Frontalis and Selenomonas Ruminantium Grown in Mixed Culture ». Dans 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.
Texte intégralJordan, Douglas B. « B-d-Xylosidase from Selenomonas ruminantium : Catalyzed Reactions with Natural and Artificial Substrates ». Dans Biotechnology for Fuels and Chemicals, 257–69. Totowa, NJ : Humana Press, 2007. http://dx.doi.org/10.1007/978-1-60327-526-2_27.
Texte intégralAizawa, Shin-Ichi. « Selenomonas ruminantium — The Authentic Lateral Flagella ». Dans The Flagellar World, 78–79. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-417234-0.00025-6.
Texte intégral