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Escherichia coli biological activity

Chen C-M, Q-Z Zhuang, Z Zhu, BL Wanner, CT Walsh (1990) Molecuar biology of carbon-phosphorus bond cleavage Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli. J Biol Chem 265 4461-4471. [Pg.591]

Characterization of Anti-Infective Biological Activity. Acute sepsis models utilizing either Escherichia coli or Staphylococcus aureus intraperitoneal challenge were developed to evaluate the anti-infective properties of PGG in mice. [Pg.47]

It soon became apparent that the biologically active forms of Vitamin Bj.2 contained the unique Co—C-a-bond, and the instability of these covalent compounds to visible light facilitated observations on the occurrence of functional corrinoids in a number of enzymes. Deoxyadenosyl-cobalamin was found to be the most abundant corrinoid in bacteria (24) and in mammalian liver (25). Methylcobalamin was found in Escherichia coli (26), calf liver and human blood plasma (27), and also in a number of Clostridia (28). [Pg.55]

Hasslacher, M., Schall, M., Hayn, M. et al. (1996) Molecular cloning of the full-length cDNA of (5)-hydroxynitrile lyase from Hevea brasiliensis. Functional expression in Escherichia coli and Saccharomyces cerevisiae and identification of an active site residue. The Journal of Biological Chemistry, 271, 5884-5891. [Pg.121]

B Aschauer, G Werner, J McCray, B Rosenwirth, H Bachmayer. Biologically active protease 3C of human rhinovirus 1A is expressed from a cloned cDNA segment in Escherichia coli. Virology 184 587-594, 1991. [Pg.320]

However, some of the studies were limited by using 2,3,7,8-TCDD concentrations in excess of its solubility in water. Only two early studies reported positive results (Hussain et al. 1972 Seiler 1973). However, the results were limited by failure to demonstrate a dose-response relationship and by low bacterial survival rates. In addition, 2,3,7,8-TCDD exposure induced reverse mutations in Escherichia coli (Hussain et al. 1972) and in Saccharomyces cerevisiae (Bronzetti et al. 1983). The conflicting data obtained in the above studies may result from technical difficulties in testing 2,3,7,8-TCDD rather than from a lack of biological activity. Testing difficulties arise from an extreme insolubility of this compound and a high toxicity observed in some test systems, which would be anticipated to result in a very narrow window for effective genotoxic doses. [Pg.330]

Farha MA, Brown ED (2010) Chemical probes of Escherichia coli uncovered through chemical-chemical interaction profiling with compounds of known biological activity. Chem Biol 17 852-862... [Pg.79]

Linemeyer, D. L., Kelly, L. J., Menke, J. G., Gimenez-Gallego, G., DiSalvo, J., and Thomas, K. A. (1987). Expression in Escherichia coli of a chemically synthesized gene for biologically active bovine fibroblast growth factor. Bio/Technology 5, 960-965. [Pg.70]

A2. Abrahamson, M., Dalbpge, H, Olafsson, I., Carlsen, S., and Grubb, A., Efficient production of native, biologically active human cystatin C by Escherichia coli. FEBS Lett. 236(1), 14—18 (1988). [Pg.90]


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See also in sourсe #XX -- [ Pg.30 , Pg.843 ]

See also in sourсe #XX -- [ Pg.843 ]




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Escherichia coli activation

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