Escherichia colt

Aerobial bacteria Yeasts and moulds Escherichia colt Enterobacteria Salmonella... 

Touati D, M Jacques, B Tardat, L Bouchard, S Despied (1995) Lethal oxidative damage and mutagenesis are generated by iron Afur mutants of Escherichia colt protective role of superoxide dismutase. J Bacterial 111-. 2305-2314. 

Ahmad D, M Sylvestre, M Sondossi (1991) Subcloning of bph genes from Pseudomonas testosteroni B-356 in Pseudomonas putida and Escherichia colt evidence for dehalogenation during initial attack on chloro-biphenyls. Appl Environ Microbiol 57 2880-2887. 

R. Mahoney, T. Wilder, and B. S. Chang, Substrate-induced thermal stabilization of lactase (Escherichia colt) in milk, Ann. N.Y. Acad. Sci., 542, 274 (1988). 

Snoep, J.L., de Graef, M.R., Westphal, A.H., de Kok, A., Teixeira, de Mattos, M.J. and Neijssel, O.M. (1993) Differences in sensitivity to NADH of purified pyruvate dehydrogenase complexes of Enterococcus faecalis, Lactococcus lactis, Azotobacter vinelandii and Escherichia colt, implications for their activity in vivo. FEMS Microbiology Letters 114, 279-283. 

Hardesty, C., Ferran, C. and DiRienzo, J. M. (1991). Plasmid-mediated sucrose metabolism in Escherichia colt characterization of scrY, the structural gene for a phosphoenolpyruvate-dependent sucrose phosphotransferase system outer membrane porin, J. Bacteriol, 173, 449-456. 

Mourez, M., Jehanno, M., Schneider, E. and Dassa, E. (1998). In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia colt modulation by ATP, Mol. Microbiol., 30, 353-363. 

Furrer, J. L., Sanders, D. N., Hook-Bamard, I. G. and McIntosh, M. A. (2002). Export of the siderophore enterobactin in Escherichia colt involvement of a 43kDa membrane exporter, Mol. Microbiol., 44, 1225-1234. 

The first, definitive identification of KDO as a constituent of the LPS from Escherichia colt 0111-B4 (and from its UDP-galactose-4-epi-merase-less mutant, J-5) was reported by Heath and Ghalambor.29 When analyzing their LPS preparations for 3,6-dideoxy-L-xyZo-hex-... 

Walker, G.C. (1984). Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia colt Microbiol. Rev. 48 60-93. 

Chen, R., and Henning, U. (1996). Aperiplasmic protein (skp) of Escherichia colt selectively binds a class of outer membrane proteins. Mol. Microbiol. 19, 1287—1294. 

Tsouloufis, T., A. Mamalaki, M. Remoundos, and S.J. Tzartos (2000). Reconstitution of conformationally dependent epitopes on the N-terminal extracellular domain of the human muscle acetylcholine receptor alpha subunit expressed in Escherichia colt implications for myasthenia gravis therapeutic approaches. Int Immunol 12(9) 1255-1265. 

The vast majority of research focused on selenium in biology (primarily in the fields of molecular biology, cell biology, and biochemistry) over the past 20 years has centered on identification and characterization of specific selenoproteins, or proteins that contain selenium in the form of selenocysteine. In addition, studies to determine the unique machinery necessary for incorporation of a nonstandard amino acid (L-selenocysteine) during translation also have been central to our understanding of how cells can utilize this metalloid. This process has been studied in bacterial models (primarily Escherichia colt) and more recently in mammals in vitro cell culture and animal models). In this work, we will review the biosynthesis of selenoproteins in bacterial systems, and only briefly review what is currently known about parallel pathways in mammals, since a comprehensive review in this area has been recently published. Moreover, we summarize the global picture of the nonspecific and specific use of selenium from a broader perspective, one that includes lesser known pathways for selenium utilization into modified nucleosides in tRNA and a labile selenium cofactor. We also review recent research on newly identified mammalian selenoproteins and discuss their role in mammalian cell biology. 

Foster DL, Fillingame RH. 1979. Energy-transducing H -ATPase of Escherichia colt purification, reconstitution and subunit composition. J Biol Chem 254 8230-6. 

The development of the concept of allosteric inhibition of enzymes began in the early 1950s but, surprisingly, not with studies on enzymes. It was discovered that addition of an amino acid to a culture of bacteria Escherichia colt)... 

NDPA has exhibited genotoxicity in bacteria Salmonella typhimurium, Escherichia colt) and mammalian cells (mouse lymphoma, Chinese hamster) and caused DNA effects (fragmentation, unscheduled synthesis, repair) in rat hepatocytes and chromosome aberrations in Chinese hamster cells. ... 

Hydrolysis of sugar nucleotides with unspecific pyrophosphatases has already been mentioned (Section 11,1, p. 310). A similar reaction is catalyzed by a bacterial enzyme specific for adenosine 5 -(a-D-glucopyranosyl pyrophosphate).459 The specific conversion of uridine 5 -(a-D-glucopyranosyl pyrophosphate) into a-D-glucopyranosyl phosphate, uridine, and inorganic phosphate was observed with an enzyme from Escherichia colt 459,460 a preparation from Bacillus subtilis can act in a similar manner461 on different sugar nucleotides. ... 

Nieboer, M., Kingma, J. Witholt, B. (1993). The alkane oxidation system of Pseudomonas oleovorans induction of the alk genes in Escherichia colt W3110 (pGEc47) affects membrane biogenesis and results in overexpression of alkane hydroxylase in a distant cytoplasmic membrane subfraction. Molecular Microbiology, 8, 1039-51. 

Mondello, F. J. (1989). Cloning and expression in Escherichia colt of Pseudomonas strain LB400 genesencodingpolychlorinated biphenyl degradation Journal ofBacteriology, 171,1725-32. 

Gruber, M Schodin, B A., Wilson, E. R., and Kranz, D. M. (1994) Efficient tumor cell lysis mediated by a bispecific single-chain antibody expressed in Escherichia colt J Immunol. 152, 5368—5374. 

Pack, P., Muller, K., Zahn, R, and Pluckthun, A (1995) Tetravalent mini-anti-bodies with high avidity assembling in Escherichia colt J. Mol. Biol 246,28—34. 

With the introduction of new technology in recombinant DNA research, it is possible to transfer via a plasmid the specific gene for a protein into another organism (usually Escherichia colt cells) and allow that organism to synthesize the desired protein (see Experiments 14 and 15). 

Bacterial cells, wet packed, 2 to 3 g. Use B subtilis, Escherichia colt, or Clostridium welchii. If lyophilized cells are available, use 0.5 g. Sahne-EDTA, 0 15 M NaCl plus 0.1 M ethylenediaminetetraacetate, pH 8... 

Escherichia colt slant, slabs, plate or liquid culture. Recommended strains are RR1, HB101, GM48, 294, SK1591,JC411Thy /ColEl, or CR34/ColEl. The strain must contain a plasmid such as ColEl, pBR322, pUR290, or the pUC series of plasmids. 

Fig. 1. Working models of the F-, V-, and A-ATPases. Model of the subunit arrange-mentin the (A) FjFo-ATP synthase from Escherichia colt, (B) vacuolar ATPase from bovine brain clathrin- coated vesicles, and (C) A A0-ATPase from Thermoplasma acidophilum. The catalytic domain is in blue, the rotor domain is in green, and the stator domain is in orange.

For comparison, several specific usage rates for industrially important bacteria and fungi are given. These range from 3.0 (Aspergillis niger) to 10.8 mmol gd, h 1 (Escherichia colt) [24]. 

Schmitt, E., Blanquet, S., and Mechulam, Y. (1996). Structure of crystalline Escherichia colt methionyl-tRNA(f)Met formyltransferase comparison with glycinamide ribonucleotide formyltransferase. EMBO J., 15, 4749-4758. 

A H Ac — CH2Ph RrHg Bacteriostatic in vitro against Escherichia colt and Srnpliyfncoccws aureus 452... 

Cartron ML, Mitchell SA, Woodhall MR et al (2007) Preliminary X-ray diffraction analysis of YcdB from Escherichia colt a novel haem-containing and Tat-secreted periplasmic protein with a potential role in iron transport. Acta Crystallogr Sect F Struct Biol Cryst Commun 63 37 11... 

The initial emphasis in analytical biotechnology was on broad safety concerns that translated into detection of host-cell components such as DNA, endotoxins, Escherichia colt proteins, and retroviral contamination.2 The detection of these impurities requires development of high-sensitivity assays that are based primarily on antibodies [e.g., enzyme-linked immunosorbent assay (ELISA) for E. coli proteins) or radioactivity (e.g., dot-blot assays for DNA detection). New developments are focused on low-sensitivity detection, characterization, and removal of undesirable target sequence variants. Bioseparations play an important role even after a product has been isolated and shown to contain a low level of contaminants for initiation of clinical studies. The focus shifts to achievement of a reproducible, large-scale manufacturing process. At this stage, analytical methods provide essential informa-... 

Parker, C., Barnell, W. O., Snoep, J. L., Ingram, L. O., and Conway, T. 1995. Characterization of the Zymomonas mobilis glucose facilitator gene product (gif) in recombinant Escherichia colt examination of the transport mechanism, kinetics and the role of glucokinase in glucose transport. Mol. Microbiol., 15, 759-802. 

A. Varma and B. 0. Palsson. Metabolic capabilities of Escherichia colt I. Synthesis of biosynthetic precursors and cofactors./. Theor. Biol., 165 477-502, 1993. 

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