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Escherichia coii

Figure 2-125. Different isovalue-based surfaces of phenylalanine a) isoelectronic density b) molecular orbitals (HOMO-LUMO) c) isopotential surface and d) isosurface of the electron cryo-microscopic volume of the ribosome of Escherichia coii. Figure 2-125. Different isovalue-based surfaces of phenylalanine a) isoelectronic density b) molecular orbitals (HOMO-LUMO) c) isopotential surface and d) isosurface of the electron cryo-microscopic volume of the ribosome of Escherichia coii.
Bacillus megaterium Bovista plumbia Escherichia coii Kiuyvera citrophila Pseudomonas melanogenum... [Pg.173]

PA S6 S06.002 EspP g.p. (Escherichia coii) Potential virulence factor that cleaves human coagulation factor V... [Pg.880]

Prostate resection, bladder resection, cystoscopy Escherichia coii Cefazolin 1 g x l Generally not recommended for patients with sterile preoperative urine cultures IB... [Pg.539]

Israeli, E Shaffer, B. T., Lighthart, B. Protection of freeze-dried Escherichia coii by trehalose upon exposure to environmental conditions. Cryobiology 30, p. 510-523, 1993... [Pg.235]

Figure 6 A general method for expressing prokaryotic tRNAs in mammalian cells, (a) A type-3 Pol III promoter, the H1 promoter, was combined with other gene elements in different ways to express the Escherichia coii amber suppressor tRNA . The GFP gene containing the TAG mutation at a permissive site serves as a fluorescence reporter for amber suppression. Translation of full-length GFP generates green fluorescence and indicates the expression of functional Escherichia coii amber suppressor tRNA in cells, (b) Total fluorescence intensity of cells transfected with constructs shown in (a). The combination in tRNA4 yields the most efficient tRNA expression. Figure 6 A general method for expressing prokaryotic tRNAs in mammalian cells, (a) A type-3 Pol III promoter, the H1 promoter, was combined with other gene elements in different ways to express the Escherichia coii amber suppressor tRNA . The GFP gene containing the TAG mutation at a permissive site serves as a fluorescence reporter for amber suppression. Translation of full-length GFP generates green fluorescence and indicates the expression of functional Escherichia coii amber suppressor tRNA in cells, (b) Total fluorescence intensity of cells transfected with constructs shown in (a). The combination in tRNA4 yields the most efficient tRNA expression.
Figure 7 The biosynthesis of unnatural amino acid p-amino-t-phenylalanine in Escherichia coii. Figure 7 The biosynthesis of unnatural amino acid p-amino-t-phenylalanine in Escherichia coii.
Escherichia coii tRNA "-Derived Suppressor tRNA... [Pg.86]

Compiicated intra-abdominai infections Caused by Escherichia coii, Ciostridium ciostridioforme, Eubacterium ientum, Peptostreptococcus sp., Bacteroides fragiiis, B. distasonis, B. ovatus, B. thetaiotaomicron, or B. uniformis. [Pg.1537]

Including secondary bacteremia from Escherichia coii (IV only). [Pg.1558]

May be effective in the treatment of acute urinary tract infections caused by susceptible strains of gram-positive and gram-negative bacteria, especially Enterobacter sp. and Escherichia coii. It usually is less effective than other antimicrobial agents in the treatment of urinary tract infections caused by bacteria other than mycobacteria. Consider using only when the more conventional therapy has failed and when the organism has demonstrated sensitivity. [Pg.1725]

Fed-Batch Cultures of Escherichia coii Cells with Oxygen-Dependent nar Promoter Systems... [Pg.177]

In contrast to the substantial work with MAO, relatively little research has been reported on the mechanism of inhibition of copper-containing amine oxidases and SSAO by cyclopropylamines. Bovine plasma amine oxidase, equine plasma amine oxidase, Escherichia coii amine oxidase, and Arthrobacter globiformis amine oxidase were inhibited by frans-2-phenylcyclopropylamine (8a) and the mode of inhibition was shown by spectral and crystal structure analyses to be competitive and reversible [36,37,129],... [Pg.683]

Contraindications Patients allergic to Escherichia coii-derived proteins... [Pg.931]

Class Synthetic antibacterial combinations with activity against Escherichia coii, Pro/eos species. Morganeiia morganii, Proteus mirahiiis, Kiebsielia species. Enterobacterspecies, Hemophiius influenzae, Streptococcus pneumoniae, Shigella flexneri, and Shigella sonnei 15 o u E c... [Pg.43]

Class Semisynthetic aminoglycoside antibiotics with activity against Pseudomonas species, Escherichia coii. Proteus species, Providencia species, Klebsiella species, Enterobacter speaes, Serratia species, Acinetobacter species, Citrobacter freundii, Staphylococcus species Aminoglycosides generally have a low level of activity against grampositive organisms Lo o u c <... [Pg.53]

Kudva, I.T., Blanch, K. and Hovde, G.J. 1998. Analysis of Escherichia coii O157 H7 in ovine or... [Pg.287]

ECW, Escherichia coii WP2 uvrA, reverse mutation - - 500 Gatehouse (1981) ... [Pg.374]

Venitt. S. Crofton-Sleigh, C. (1981) Mutagenicity of 42 coded compounds in a bacterial assay using Escherichia coii and Salmonella typhimurium (Chester Beatty Research Institute). In de Serres, F.J. Ashby, J., eds. Progress in Mutation Research, Vol. 1. Evaluation of Short-Term Tests for Carcinogens. Report of the International Collaborative Program, Amsterdam, Elsevier/North-Holland, pp. 351-360... [Pg.382]

Zielenska, M., Horsfall, M.J. Glickman. B.W. (1989) The dissimilar mutational consequences of SnI and 8 2 DNA alkylation pathways clues from the mutational specificity of dimethyl-sulphate in the lad gene of Escherichia coii. Mutagenesis, 4, 230-234... [Pg.588]

ECW, Escherichia coii WP2 wvrA, reverse mutation + + 10% atm JETOC (1997)... [Pg.743]

ECF, Escherichia coii, forward mutation - NT NG Quinto Radman (1987)... [Pg.1268]


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See also in sourсe #XX -- [ Pg.182 ]

See also in sourсe #XX -- [ Pg.370 ]

See also in sourсe #XX -- [ Pg.30 , Pg.59 , Pg.72 , Pg.200 , Pg.221 , Pg.222 ]




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