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Artículos de revistas sobre el tema "Selenomonas ruminantium"

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Publicado: 4 de junio de 2021
Última modificación: 28 de enero de 2023

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1

Michel, Tomas A., and Joan M. Macy. "Ferredoxin from Selenomonas ruminantium." Archives of Microbiology 153, no. 5 (April 1990): 518–20. http://dx.doi.org/10.1007/bf00248437.

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2

Kalmokoff, M. L., J. W. Austin, M. F. Whitford, and R. M. Teather. "Characterization of a major envelope protein from the rumen anaerobeSelenomonas ruminantiumOB268." Canadian Journal of Microbiology 46, no. 4 (April 1, 2000): 295–303. http://dx.doi.org/10.1139/w99-149.

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Cell envelopes from the Gram-negative staining but phylogenetically Gram-positive rumen anaerobe Selenomonas ruminantium OB268 contained a major 42 kDa heat modifiable protein. A similarly sized protein was present in the envelopes of Selenomonas ruminantium D1 and Selenomonas infelix. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of Triton X-100 extracted cell envelopes from S. ruminantium OB268 showed that they consisted primarily of the 42 kDa protein. Polyclonal antisera produced against these envelopes cross-reacted only with the 42 kDa major envelope proteins in both S. rumin
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3

Pristas, Peter, and 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 (April 1, 2005): 315–18. http://dx.doi.org/10.1139/w05-004.

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Molecular analysis of isolates of the rumen bacterium Selenomonas ruminantium revealed a high variety and frequency of site-specific (restriction) endonucleases. While all known S. ruminantium restriction and modification systems recognize hexanucleotide sequences only, consistently low counts of both 6-bp and 4-bp palindromes were found in DNA sequences of S. ruminantium. Statistical analysis indicated that there is some correlation between the degree of underrepresentation of tetranucleotide words and the number of known restriction endonucleases for a given sequence. Control analysis showed
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4

Wiryawan, KG, and 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.

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When sheep were acutely fed a grain diet, ruminal pH rapidly dropped to less than 5.0, lactic acid exceeded 100 mM and clinical symptoms of acidosis were evident within 24 h. When acute grain feeding was preceeded by inoculation of the rumen with 108 cfu of Selenomonas ruminantium subsp. lactilytica strain JDB201, ruminal lactate was undetectable and ruminal pH was stabilized at 6.3-6.5 for up to 24 h. Inoculation of the rumen with a mixture of 108 cfu each of Selenomonas ruminantium subsp. lactilytica strain JDB201 and Megasphaera elsdenii strain JDB301 was shown to be more effective than Sel
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5

Haya, Shohei, Yuya Tokumaru, Naoki Abe, Jun Kaneko, and Shin-ichi Aizawa. "Characterization of Lateral Flagella of Selenomonas ruminantium." Applied and Environmental Microbiology 77, no. 8 (February 18, 2011): 2799–802. http://dx.doi.org/10.1128/aem.00286-11.

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ABSTRACTSelenomonas ruminantiumproduces a tuft of flagella near the midpoint of the cell body and swims by rotating the cell body along the cell's long axis. The flagellum is composed of a single kind of flagellin, which is heavily glycosylated. The hook length ofS. ruminantiumis almost double that ofSalmonella.
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6

Fecskeová, Lívia, Peter Pristaš, and Peter Javorský. "Cloning and characterization of cobA, one of vitamin B12 biosynthesis pathway genes from Selenomonas ruminantium." Nova Biotechnologica et Chimica 10, no. 2 (August 31, 2021): 131–35. http://dx.doi.org/10.36547/nbc.1122.

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Bacterial biosynthesis of vitamin B12 can occur via either aerobic or anaerobic route. While the aerobic pathway has been fully elucidated and understood, less is known about the anaerobic pathway. Selenomonas ruminantium is thought to be the main producer of this vitamin in rumen environment and must use the anaerobic pathway. In our work we found one of the genes of vitamin B12 biosynthetic pathway of S. ruminantium, encoding for the cobalamin adenosyltransferase, enzyme taking part at the last steps of the synthesis process. Deduced amino acid sequence showed the highest similarity to cobal
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7

Nisbet, David J., and Scott A. Martin. "Factors affecting L-lactate utilization by Selenomonas ruminantium." Journal of Animal Science 72, no. 5 (May 1, 1994): 1355–61. http://dx.doi.org/10.2527/1994.7251355x.

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8

Williams, D. K., and 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.

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9

Brooker, J. D., and 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.

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10

Kopecny, J., V. Kostyukovsky, and 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.

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11

Cotta, MA, and TR Whitehead. "Xylooligosaccharide utilization by the ruminal bacterium Selenomonas ruminantium." Reproduction Nutrition Development 37, Suppl. 1 (1997): 51–52. http://dx.doi.org/10.1051/rnd:19970732.

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12

Fliegerová, Benada, and Flint. "Large plasmids in ruminal strains of Selenomonas ruminantium." Letters in Applied Microbiology 26, no. 4 (April 1998): 243–47. http://dx.doi.org/10.1046/j.1472-765x.1998.00299.x.

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13

Pristas, P., K. Fliegerova, and P. Javorsky. "Two restriction endonucleases in Selenomonas ruminantium subsp. lactilytica." Letters in Applied Microbiology 27, no. 2 (August 1998): 83–85. http://dx.doi.org/10.1046/j.1472-765x.1998.00392.x.

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14

Martin, Scott A. "Hexose Phosphorylation by the Ruminal Bacterium Selenomonas ruminantium." Journal of Dairy Science 79, no. 4 (April 1996): 550–56. http://dx.doi.org/10.3168/jds.s0022-0302(96)76399-3.

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15

Kopecny, J., V. Kostyukovsky, and K. Fliegerova. "Electroporation of G+ host plasmids into Selenomonas ruminantium." Annales de Zootechnie 45, Suppl. 1 (1996): 356. http://dx.doi.org/10.1051/animres:19960685.

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16

de Vries, Wytske, Willemina M. C. van Wijck-Kapteyn, and S. K. H. Oosterhuis. "The Presence and Function of Cytochromes in Selenomonas ruminantium, Anaerovibrio lipolytica and Veillonella alcalescens." Microbiology 81, no. 1 (January 1, 2000): 69–78. http://dx.doi.org/10.1099/00221287-81-1-69.

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Strains of Selenomonas ruminantium, Anaerovibrio lipolytica and Veillonella alcalescens contained cytochrome b. Peaks corresponding to cytochromes a and a carbon monoxide-binding pigment were also observed. By means of dual-wavelength experiments with crude membrane fractions it was established that cytochrome b functioned in anaerobic electron transport to fumarate. In V. alcalescens and one strain of S. ruminantium which reduced nitrate, anaerobic electron transport to nitrate was found. Glycerol 1-phosphate and NADH were active as hydrogen donors for cytochrome b reduction in glycerol-grown
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17

Matte, Allan, Cecil W. Forsberg, and Ann M. Verrinder Gibbins. "Enzymes associated with metabolism of xylose and other pentoses by Prevotella (Bacteroides) ruminicola strains, Selenomonas ruminantium D, and Fibrobacter succinogenes S85." Canadian Journal of Microbiology 38, no. 5 (May 1, 1992): 370–76. http://dx.doi.org/10.1139/m92-063.

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Prevotella (Bacteroides) ruminicola strains B14 and S23 and Selenomonas ruminantium strain D used xylose as the sole source of carbohyrate for growth, whereas Fibrobacter succinogenes was unable to metabolize xylose. Prevotella ruminicola strain B14 exhibited transport activity for xylose. In contrast, F. succinogenes lacked typical xylose uptake activity but did exhibit low binding potential for the sugar. Prevotella ruminicola strains B14 and S23 as well as S. ruminantium D showed low xylose isomerase activities but higher xylulokinase activities, using assays that gave high activities for t
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18

Cotta, Michael A., and Terence R. Whitehead. "Xylooligosaccharide Utilization by the Ruminal Anaerobic Bacterium Selenomonas ruminantium." Current Microbiology 36, no. 4 (April 1, 1998): 183–89. http://dx.doi.org/10.1007/s002849900291.

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19

Michel, Tomas A., and Joan M. Macy. "Preparation of spheroplasts from the strict anaerobe Selenomonas ruminantium." Journal of Microbiological Methods 11, no. 1 (February 1990): 37–41. http://dx.doi.org/10.1016/0167-7012(90)90045-8.

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20

Evans, J. D., and S. A. Martin. "Factors affecting lactate and malate utilization by Selenomonas ruminantium." Applied and environmental microbiology 63, no. 12 (1997): 4853–58. http://dx.doi.org/10.1128/aem.63.12.4853-4858.1997.

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21

Bishop, Richard, Moses Obura, David Odongo, and Agnes Odenyo. "Specific PCR Assay for a Tannin-Tolerant Selenomonas ruminantium Isolate, Derived from Helicase Coding Sequences." Applied and Environmental Microbiology 70, no. 5 (May 2004): 3180–82. http://dx.doi.org/10.1128/aem.70.5.3180-3182.2004.

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ABSTRACT Sequences from a tannin-tolerant Selenomonas ruminantium isolate (EAT2) that hydrolyzes gallic acid were identified. Two exhibited identity to helicases with a wide phylogenetic distribution. PCR amplification by using primers from one helicase gene detected 2,000 to 5,000 EAT2 genome equivalents but did not amplify total gastrointestinal microbial DNA of nine other ungulate species.
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22

D'Silva, C. G., H. D. Bae, L. J. Yanke, K. J. Cheng, and L. B. Selinger. "Localization of phytase in Selenomonas ruminantium and Mitsuokella multiacidus by transmission electron microscopy." Canadian Journal of Microbiology 46, no. 4 (April 1, 2000): 391–95. http://dx.doi.org/10.1139/w00-001.

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The localization of phytase (myo-inositol-hexaphosphate phosphohydrolase) in the ruminal bacteria, Selenomonas ruminantium JY35 and Mitsuokella multiacidus 46/5(2), was determined with transmission electron microscopy. Phosphate produced from the enzymatic dephosphorylation of the calcium salt of phytic acid is precipitated as calcium phosphate. The calcium is then replaced with lead to produce electron-dense lead phosphate. This deposition of lead phosphate localized phytase in S. ruminantium JY35 and M. multiacidus 46/5(2) to the outer membrane, and confirmed intracellular expression of the
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23

Caldwell, Daniel R. "Effects of methanol on the growth of gastrointestinal anaerobes." Canadian Journal of Microbiology 35, no. 2 (February 1, 1989): 313–17. http://dx.doi.org/10.1139/m89-047.

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The effects of methanol on the growth of representative, predominant, anaerobic gut bacteria were studied. Growth yields and rates were determined in a base medium to which methanol was added to produce media with methanol concentrations varying, in twofold steps, over a concentration range of 0.01 to 25%, by volume. The growth of many of the organisms was completely inhibited by a methanol concentration equal to, or less than, 6.2%. Isolates representing cellulolytic species were completely inhibited at a methanol concentration of 3.1%, and inhibitory effects on the yield of some cellulolytic
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24

Piña-Gónzalez, Laura, Juan Miranda-Ríos, Rogelio Alejandro Alonso-Morales, Otoniel Maya, Luis Corona, and Claudia Cecilia Márquez-Mota. "PSXIV-15 Metagenomic sequencing of rumen microorganisms of cattle fed a corn stover-based diet." Journal of Animal Science 97, Supplement_3 (December 2019): 441–44. http://dx.doi.org/10.1093/jas/skz258.873.

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Abstract Worldwide, there is a need to discover new microorganisms that efficiently degrade lignocellulosic complexes that would help to improve the digestibility of low-quality agricultural byproducts. The aim of the study was to evaluate the effects of a corn stover-based diet (CSD) on rumen bacteria. Ruminal fluid of 6 Holstein cows (595 ± 96 kg) was collected during two periods. During first period, animals were consuming a diet based on corn silage and oat hay (DB), mineral premix and water ad libitum (50:50, DM). In second period, animals were provided a CSD (100% DM), mineral premix and
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25

Takatsuka, Yumiko, Yoshihiro Yamaguchi, Minenobu Ono, and Yoshiyuki Kamio. "Gene Cloning and Molecular Characterization of Lysine Decarboxylase from Selenomonas ruminantiumDelineate Its Evolutionary Relationship to Ornithine Decarboxylases from Eukaryotes." Journal of Bacteriology 182, no. 23 (December 1, 2000): 6732–41. http://dx.doi.org/10.1128/jb.182.23.6732-6741.2000.

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ABSTRACT Lysine decarboxylase (LDC; EC 4.1.1.18 ) from Selenomonas ruminantium comprises two identical monomeric subunits of 43 kDa and has decarboxylating activities toward both l-lysine andl-ornithine with similar Km andVmax values (Y. Takatsuka, M. Onoda, T. Sugiyama, K. Muramoto, T. Tomita, and Y. Kamio, Biosci. Biotechnol. Biochem. 62:1063–1069, 1999). Here, the LDC-encoding gene (ldc) of this bacterium was cloned and characterized. DNA sequencing analysis revealed that the amino acid sequence of S. ruminantium LDC is 35% identical to those of eukaryotic ornithine decarboxylases (ODCs; EC
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26

Martin, S. A., and R. G. Dean. "Characterization of a plasmid from the ruminal bacterium Selenomonas ruminantium." Applied and Environmental Microbiology 55, no. 12 (1989): 3035–38. http://dx.doi.org/10.1128/aem.55.12.3035-3038.1989.

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27

Gilmour, M., H. J. Flint, and W. J. Mitchell. "Multiple lactate dehydrogenase activities of the rumen bacterium Selenomonas ruminantium." Microbiology 140, no. 8 (August 1, 1994): 2077–84. http://dx.doi.org/10.1099/13500872-140-8-2077.

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28

Pristas, P., I. Vanat, N. Kostrabova, and P. Javorsky. "Variability of endonucleolytic activity within natural population of Selenomonas ruminantium." Reproduction Nutrition Development 37, Suppl. 1 (1997): 75–76. http://dx.doi.org/10.1051/rnd:19970759.

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29

MARTIN, S. A., and J. B. RUSSELL. "Mechanisms of Sugar Transport in the Rumen Bacterium Selenomonas ruminantium." Microbiology 134, no. 3 (March 1, 1988): 819–27. http://dx.doi.org/10.1099/00221287-134-3-819.

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30

Chu, Hsing-Mao, Rey-Ting Guo, Ting-Wan Lin, Chia-Cheng Chou, Hui-Lin Shr, Hui-Lin Lai, Tsung-Yin Tang, Kuo-Joan Cheng, Brent L. Selinger, and Andrew H. J. Wang. "Structures of Selenomonas ruminantium Phytase in Complex with Persulfated Phytate." Structure 12, no. 11 (November 2004): 2015–24. http://dx.doi.org/10.1016/j.str.2004.08.010.

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31

Al-Khaldi, Sufian F., Lawren L. Durocher, and Scott A. Martin. "Deoxyribonuclease Activity in Selenomonas ruminantium , Streptococcus bovis , and Bacteroides ovatus." Current Microbiology 41, no. 3 (September 13, 2000): 182–86. http://dx.doi.org/10.1007/s002840010115.

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32

Yamaguchi, Yoshihiro, Yumiko Takatsuka, and Yoshiyuki Kamio. "Two Segments in Bacterial Antizyme P22 Are Essential for Binding and Enhance Degradation of Lysine/Ornithine Decarboxylase in Selenomonas ruminantium." Journal of Bacteriology 190, no. 1 (October 26, 2007): 442–46. http://dx.doi.org/10.1128/jb.01429-07.

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ABSTRACT In Selenomonas ruminantium, a strictly anaerobic and gram-negative bacterium, the degradation of lysine/ornithine decarboxylase (LDC/ODC) by ATP-requiring protease(s) is accelerated by the binding of P22, which is a ribosomal protein of this strain. Amino acid sequence alignment of S. ruminantium P22 with the L10 ribosomal proteins of gram-positive and -negative bacteria showed that P22 has a 5-residue K101NKLD105 segment and an 11-residue G160VIRNAVYVLD170 segment, both of which are lacking in L10 in any other gram-positive and gram-negative bacteria reported. To elucidate whether th
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33

Heinrichová, Kveta, Július Heinrich, Mária Dzúrová та Alexander Ziolecki. "Mode of Action and Partial Purification of the Active Centre of exo-Poly-α-D-galacturonosidase from Selenomonas ruminantium". Collection of Czechoslovak Chemical Communications 58, № 3 (1993): 681–92. http://dx.doi.org/10.1135/cccc19930681.

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In the presented paper are summarized results of the study of the mode of action, dimensions and arrangement of the active centre of the exo-poly-α-D-galacturonosidase, (poly(1,4-α-D-galactosiduronate) digalacturonohydrolase, E.C. 3.2.1.82) produced by the bacteria Selenomonas ruminantium. With this aim we determined experimentally values of Michaelis constants and limiting rates for the catalytic hydrolysis of linear oligo(D-galactosiduronates) of the degree of polymeration in the range of 3 to 8, at pH 7.0 and the temperature 30 °C. We calculated molecular activities k0 and parameters k0/Km
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34

Grochowska, Sylwia, Włodzimierz Nowak, Małgorzata Lasik-Kurdyś, Robert Mikuła, and Jacek Nowak. "The effect of Saccharomyces cerevisiae on in vitro growth and fermentation of Selenomonas ruminantium and Megasphaera elsdenii." Roczniki Naukowe Polskiego Towarzystwa Zootechnicznego 13, no. 3 (September 29, 2017): 9–22. http://dx.doi.org/10.5604/01.3001.0010.5453.

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Stimulation of lactate utilization by Selenomonas ruminantium and Megasphaera elsdenii may help in reducing problems associated with rumen acidosis. The objective of this study was to determine the effect of a Saccharomyces cerevisiae live culture and Saccharomyces cerevisiae fermentation products on in vitro growth and fermentation of lactate-utilizing ruminal bacteria, S. ruminantium (ATCC 19205) and M. elsdenii (ATCC 25940). The cultures were run for 0, 6, 12, 24 and 48 h under anaerobic conditions on a growth medium supplemented with a yeast live culture (SC) or with yeast fermentation pro
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35

Cotta, M. A. "Utilization of nucleic acids by Selenomonas ruminantium and other ruminal bacteria." Applied and Environmental Microbiology 56, no. 12 (1990): 3867–70. http://dx.doi.org/10.1128/aem.56.12.3867-3870.1990.

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36

Silley, P., and D. G. Armstrong. "Metabolism of the rumen bacterium Selenomonas ruminantium grown in continuous culture." Letters in Applied Microbiology 1, no. 3 (March 1985): 53–55. http://dx.doi.org/10.1111/j.1472-765x.1985.tb01488.x.

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37

Dean, R. G., S. A. Martin, and C. Carver. "Isolation of plasmid DNA from the ruminal bacterium Selenomonas ruminantium HD4." Letters in Applied Microbiology 8, no. 2 (February 1989): 45–48. http://dx.doi.org/10.1111/j.1472-765x.1989.tb00220.x.

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38

Pristas, Peter, Jozef Ivan, and Peter Javorsky. "Structural instability of small rolling circle replication plasmids from Selenomonas ruminantium." Plasmid 64, no. 2 (September 2010): 74–78. http://dx.doi.org/10.1016/j.plasmid.2010.04.005.

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39

Nakamura, Mutsumi, Takafumi Nagamine, Koretsugu Ogata, Kiyoshi Tajima, and Rustem I. Aminov. "Sequence Analysis of Small Cryptic Plasmids Isolated from Selenomonas ruminantium S20." Current Microbiology 38, no. 2 (February 1, 1999): 107–12. http://dx.doi.org/10.1007/s002849900412.

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40

Jordan, Douglas B., Xin-Liang Li, Christopher A. Dunlap, Terence R. Whitehead та Michael A. Cotta. "β-d-Xylosidase from Selenomonas ruminantium of glycoside hydrolase family 43". Applied Biochemistry and Biotechnology 137-140, № 1-12 (квітень 2007): 93–104. http://dx.doi.org/10.1007/s12010-007-9042-6.

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41

Ricke, S. C., and D. M. Schaefer. "An ascorbate-reduced medium for nitrogen metabolism studies with Selenomonas ruminantium." Journal of Microbiological Methods 11, no. 3-4 (July 1990): 219–27. http://dx.doi.org/10.1016/0167-7012(90)90058-e.

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42

Skene, I. K., and J. D. Brooker. "Characterization of Tannin Acylhydrolase Activity in the Ruminal Bacterium Selenomonas Ruminantium." Anaerobe 1, no. 6 (December 1995): 321–27. http://dx.doi.org/10.1006/anae.1995.1034.

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43

Fliegerova, Katerina, Sylvie Pazoutova, Peter Pristas, and Harry J. Flint. "Highly Conserved DNA Sequence Present in Small Plasmids from Selenomonas ruminantium." Plasmid 44, no. 1 (July 2000): 94–99. http://dx.doi.org/10.1006/plas.2000.1464.

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44

Ghali, M. B., P. T. Scott, G. A. Alhadrami, and R. A. M. Al Jassim. "Identification and characterisation of the predominant lactic acid-producing and lactic acid-utilising bacteria in the foregut of the feral camel (Camelus dromedarius) in Australia." Animal Production Science 51, no. 7 (2011): 597. http://dx.doi.org/10.1071/an10197.

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The camel is emerging as a new and important animal in the Australian livestock industry. However, little is known regarding the microbial ecosystem of the gastrointestinal tract of this ruminant-like animal. This study was carried out to determine the diversity of lactic acid-producing and lactic acid-utilising bacteria in the foregut of the feral camel (Camelus dromedarius) in Australia. Putative lactic acid bacteria were isolated from the foregut contents of camels by culturing on De Man, Rogosa, Sharpe and lactic acid media. Identification of representative isolates was based on the analys
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45

Rasmussen, M. A. "Isolation and characterization of Selenomonas ruminantium strains capable of 2-deoxyribose utilization." Applied and Environmental Microbiology 59, no. 7 (1993): 2077–81. http://dx.doi.org/10.1128/aem.59.7.2077-2081.1993.

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46

Gilmour, M., W. J. Mitchell, and H. J. Flint. "Genetic transfer of lactate-utilizing ability in the rumen bacterium Selenomonas ruminantium." Letters in Applied Microbiology 22, no. 1 (January 1996): 52–56. http://dx.doi.org/10.1111/j.1472-765x.1996.tb01107.x.

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47

Sawanon, Suriya, Satoshi Koike, and Yasuo Kobayashi. "Evidence for the possible involvement of Selenomonas ruminantium in rumen fiber digestion." FEMS Microbiology Letters 325, no. 2 (October 21, 2011): 170–79. http://dx.doi.org/10.1111/j.1574-6968.2011.02427.x.

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Terrasan, César Rafael Fanchini, Caio Casale Aragon, Douglas Chodi Masui, Benevides Costa Pessela, Gloria Fernandez-Lorente, Eleonora Cano Carmona та Jose Manuel Guisan. "β-xylosidase from Selenomonas ruminantium: Immobilization, stabilization, and application for xylooligosaccharide hydrolysis". Biocatalysis and Biotransformation 34, № 4 (3 липня 2016): 161–71. http://dx.doi.org/10.1080/10242422.2016.1247817.

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Sprincova, Adriana, Peter Javorsky, and Peter Pristas. "pSRD191, a new member of RepL replicating plasmid family from Selenomonas ruminantium." Plasmid 54, no. 1 (July 2005): 39–47. http://dx.doi.org/10.1016/j.plasmid.2004.11.004.

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Hausinger, R. P. "Purification of a nickel-containing urease from the rumen anaerobe Selenomonas ruminantium." Journal of Biological Chemistry 261, no. 17 (June 1986): 7866–70. http://dx.doi.org/10.1016/s0021-9258(19)57483-x.

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