Comparative Activity of Moxifloxacin in Vitro Against Obligately Anaerobic Bacteria

2000 ◽  
Vol 19 (3) ◽  
pp. 228-232 ◽  
Author(s):  
G. Ackermann ◽  
R. Schaumann ◽  
B. Pless ◽  
M. C. Claros ◽  
E. J. C. Goldstein ◽  
...  
2004 ◽  
Vol 48 (6) ◽  
pp. 2280-2282 ◽  
Author(s):  
Grit Ackermann ◽  
Birgit Löffler ◽  
Daniela Adler ◽  
Arne C. Rodloff

ABSTRACT Clostridium difficile remains the major cause of nosocomial diarrhea. Reports on impaired susceptibility of C. difficile to metronidazole and vancomycin and frequent relapses of patients after therapy necessitate the search for new substances. With this study, the activity of OPT-80, a new macrocycle, against 207 C. difficile strains and against other obligately anaerobic bacteria was tested. OPT-80 showed high in vitro activity against all C. difficile strains tested.


2001 ◽  
Vol 45 (6) ◽  
pp. 1896-1899 ◽  
Author(s):  
Niels Kleinkauf ◽  
Grit Ackermann ◽  
Reiner Schaumann ◽  
Arne C. Rodloff

ABSTRACT The in vitro activity of gemifloxacin was compared to that of other quinolone and nonquinolone antimicrobials against 204 anaerobes by the agar dilution technique. The data indicate that gemifloxacin has a rather selective anaerobic activity. Most Peptostreptococcus, Porphyromonas, and Fusobacterium species are susceptible, while gemifloxacin's activity against other gram-negative anaerobes appears to be variable.


2000 ◽  
Vol 16 (3) ◽  
pp. 225-232 ◽  
Author(s):  
Reiner Schaumann ◽  
Grit Ackermann ◽  
Baerbel Pless ◽  
Marina C Claros ◽  
Ellie J.C Goldstein ◽  
...  

1999 ◽  
Vol 43 (11) ◽  
pp. 2783-2786 ◽  
Author(s):  
Reiner Schaumann ◽  
Grit Ackermann ◽  
Baerbel Pless ◽  
Marina C. Claros ◽  
Arne C. Rodloff

ABSTRACT The activity of the new fluoroquinolone gatifloxacin was compared with those of other quinolones and antimicrobial agents of other classes against 294 anaerobes by the broth microdilution technique. For all strains tested, gatifloxacin MICs at which 50 and 90% of the isolates were inhibited were 0.5 and 2 mg/liter, respectively, and were 3 to 4 dilution steps lower than, e.g., ciprofloxacin.


Drugs ◽  
1995 ◽  
Vol 49 (Supplement 2) ◽  
pp. 233-234
Author(s):  
Carl Erik Nord ◽  
Ann Lindmark ◽  
Ingela Persson

1996 ◽  
Vol 38 (2) ◽  
pp. 271-281 ◽  
Author(s):  
K. E. Bowker ◽  
M. Wootton ◽  
H. A. Holt ◽  
D. S. Reeves ◽  
A. P. MacGowan

1983 ◽  
Vol 57 (1) ◽  
pp. 31-36 ◽  
Author(s):  
Suman Gupta ◽  
J. C. Katiyar

AbstractThe activity, in terms of speed of action, of three anticestode drugs against Hymenolepis nana, both in vivo and in vitro, was investigated. Praziquantel was most effective in vivo, but had little action on adult worms and cysticercoids in vitro. Niclosamide, the least effective in vivo, was highly toxic in vitro. Compound 77–6 killed adult worms and cysticercoids in vitro in 10 min and 15 min respectively at 1000 μg/ml of drug concentration, but its in viro effect was intermediate between that of praziquantel and niclosamide.


2005 ◽  
Vol 71 (3) ◽  
pp. 1522-1530 ◽  
Author(s):  
Amy M. Grunden ◽  
Francis E. Jenney ◽  
Kesen Ma ◽  
Mikyoung Ji ◽  
Michael V. Weinberg ◽  
...  

ABSTRACT A scheme for the detoxification of superoxide in Pyrococcus furiosus has been previously proposed in which superoxide reductase (SOR) reduces (rather than dismutates) superoxide to hydrogen peroxide by using electrons from reduced rubredoxin (Rd). Rd is reduced with electrons from NAD(P)H by the enzyme NAD(P)H:rubredoxin oxidoreductase (NROR). The goal of the present work was to reconstitute this pathway in vitro using recombinant enzymes. While recombinant forms of SOR and Rd are available, the gene encoding P. furiosus NROR (PF1197) was found to be exceedingly toxic to Escherichia coli, and an active recombinant form (rNROR) was obtained via a fusion protein expression system, which produced an inactive form of NROR until cleavage. This allowed the complete pathway from NAD(P)H to the reduction of SOR via NROR and Rd to be reconstituted in vitro using recombinant proteins. rNROR is a 39.9-kDa protein whose sequence contains both flavin adenine dinucleotide (FAD)- and NAD(P)H-binding motifs, and it shares significant similarity with known and putative Rd-dependent oxidoreductases from several anaerobic bacteria, both mesophilic and hyperthermophilic. FAD was shown to be essential for activity in reconstitution assays and could not be replaced by flavin mononucleotide (FMN). The bound FAD has a midpoint potential of −173 mV at 23°C (−193 mV at 80°C). Like native NROR, the recombinant enzyme catalyzed the NADPH-dependent reduction of rubredoxin both at high (80°C) and low (23°C) temperatures, consistent with its proposed role in the superoxide reduction pathway. This is the first demonstration of in vitro superoxide reduction to hydrogen peroxide using NAD(P)H as the electron donor in an SOR-mediated pathway.


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