Plasma proteins and leukocyte kinetics of turtles (Podocnemis unifilis (Troschel, 1848)) inoculated with inactivated Escherichia coli

2019 ◽  
Vol 29 (1) ◽  
pp. 305-310
Author(s):  
Maria Beatriz Fraga Costa ◽  
Regina Mamede Costa ◽  
Marcillo Altoé Boldrin ◽  
Evandro Pereira Neto ◽  
Paulo Dias Ferreira Júnior ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Plasma Proteins ◽  
Podocnemis Unifilis ◽  
Kinetics Of

scholarly journals Kinetics of electron transfer from NADH to the Escherichia coli nitric oxide reductase flavorubredoxin

FEBS Journal ◽  
2006 ◽  
Vol 274 (3) ◽  
pp. 677-686 ◽  
Author(s):  
João B. Vicente ◽  
Francesca M. Scandurra ◽  
João V. Rodrigues ◽  
Maurizio Brunori ◽  
Paolo Sarti ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Escherichia Coli ◽  
Electron Transfer ◽  
Nitric Oxide Reductase ◽  
Kinetics Of

scholarly journals Membrane-permeable luciferin esters for assay of firefly luciferase in live intact cells

1991 ◽  
Vol 276 (3) ◽  
pp. 637-641 ◽  
Author(s):  
F F Craig ◽  
A C Simmonds ◽  
D Watmore ◽  
F McCapra ◽  
M R H White
Keyword(s):  
Escherichia Coli ◽  
Mammalian Cells ◽  
Firefly Luciferase ◽  
Luciferase Expression ◽  
Intact Cells ◽  
Cos Cells ◽  
Escherichia Coli Cells ◽  
Luminescent Signal ◽  
The Difference ◽  
Kinetics Of

Five esters of luciferin were synthesized and compared with native luciferin as substrates for firefly luciferase expressed in live intact mammalian cells. The esters themselves were not substrates for purified luciferase, but four were substrates for a purified esterase and all appeared to be hydrolysed to luciferin within mammalian cells. At a substrate concentration of 0.01 mM, the peak luminescence from the cos cells expressing luciferase was up to 6-fold greater with the esters than with unmodified luciferin. At 0.1 mM, the difference between luciferin and the esters was decreased. The kinetics of the luminescent signal with the different luciferin esters varied significantly, indicating possible differences in the rates of uptake, breakdown and enzyme inhibition. The esters did not support luminescence from Escherichia coli cells expressing firefly luciferase, suggesting a lack of appropriate esterase activity in this particular strain. The esters could be useful for the assay of luciferase expression in intact mammalian cells when luciferin levels are limiting, for example in tissues, and in plants. Alternative luciferin derivatives may allow further improvements in sensitivity.

scholarly journals Characterization of the Two Mycobacterium tuberculosis recA Promoters

2003 ◽  
Vol 185 (20) ◽  
pp. 6005-6015 ◽  
Author(s):  
Krishna K. Gopaul ◽  
Patricia C. Brooks ◽  
Jean-François Prost ◽  
Elaine O. Davis
Keyword(s):  
Escherichia Coli ◽  
Dna Damage ◽  
Mycobacterium Tuberculosis ◽  
Promoter Activity ◽  
The Other ◽  
Expression Level ◽  
Promoter Elements ◽  
Kinetics Of

ABSTRACT The recA gene of Mycobacterium tuberculosis is unusual in that it is expressed from two promoters, one of which, P1, is DNA damage inducible independently of LexA and RecA, while the other, P2, is regulated by LexA in the classical way (E. O. Davis, B. Springer, K. K. Gopaul, K. G. Papavinasasundaram, P. Sander, and E. C. Böttger, Mol. Microbiol. 46:791-800, 2002). In this study we characterized these two promoters in more detail. Firstly, we localized the promoter elements for each of the promoters, and in so doing we identified a mutation in each promoter which eliminates promoter activity. Interestingly, a motif with similarity to Escherichia coli σ70 −35 elements but located much closer to the −10 element is important for optimal expression of P1, whereas the sequence at the −35 location is not. Secondly, we found that the sequences flanking the promoters can have a profound effect on the expression level directed by each of the promoters. Finally, we examined the contribution of each of the promoters to recA expression and compared their kinetics of induction following DNA damage.

The preparation and kinetics of immobilised penicillin amidase from Escherichia coli

1972 ◽  
Vol 284 (1) ◽  
pp. 278-284 ◽  
Author(s):  
D. Warburton ◽  
K. Balasingham ◽  
P. Dunnill ◽  
M.D. Lilly
Keyword(s):  
Escherichia Coli ◽  
Penicillin Amidase ◽  
Kinetics Of
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