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Results for “FUSIDIC ACID”

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At least 1,063 records · Page 59Linked to original sources
PubMed1977

Hepatic uptake and biliary excretion of a bile salt analog : glycodihydrofusidate.

Glyco-24, 25-dihydrofusidate is efficiently excreted in the bile by the liver. This compound partially inhibits hepatobiliary transport of bile salts and bilirubin. In order to determine if bile salts and glycodihydrofusidate share common pathways at the hepatocyte level, we studied the effect of sodium dehydrocholate on the blood clearance of glycodihydrofusidate. Two groups of rats were perfused, controls with 0.15M NaCl, and test animals with 10 micronmol + min-(1) + kg(1) of dehydrocholate; both groups received 1 micronCi of 14C-glycodihydrofusidate intravenously. Carotid blood was removed every minute and the disappearance of radioactivity from the blood was monitored. The results are consisgent with a theoretical model of two compartments. The experimental curves were fit to the sum of exponentials.

Animals↗
PubMed1989

Topical antibiotics in the treatment of superficial skin infections in general practice--a comparison of mupirocin with sodium fusidate.

A total of 413 eligible patients took part in an observer-blind randomised multicentre clinical trial in order to compare the clinical and bacteriological efficacy of mupirocin (Bactroban) ointment with sodium fusidate (Fucidin) ointment for treating superficial skin infections seen in general practice. Mupirocin was applied twice daily and sodium fusidate thrice daily for a period of 7 days. Both treatments were similarly effective with 97% patients treated with mupirocin and 93% patients treated with sodium fusidate responding. Mupirocin was significantly more effective in the treatment of acute primary skin infections and in the treatment of a subgroup of patients with impetigo (P less than 0.01). Of the organisms detected before treatment began, 93% were not found after treatment with mupirocin compared with 89% after treatment with sodium fusidate. Staphylococcus aureus and/or beta-haemolytic streptococci appeared to be eliminated in significantly more patients treated with mupirocin (96%) compared with those treated with sodium fusidate (88%), (P = 0.03). Both treatments were well tolerated.

Administration, Topical↗
PubMed1974

Marker discrimination and mutagen-induced alterations in pneumococcal transformation.

Nitrous acid-induced and hydroxylamine-induced chemical alterations in transforming DNA result in the loss of biological activity and in mutagenesis. The function responsible for the discrimination between high efficiency and low efficiency markers in pneumococcal transformation, and for the elimination of a substantial fraction of spontaneously occurring mutational events, does not appear to act on integrated DNA carrying these chemical alterations. The chemical modifications result in mutations that are evident among bacteria transformed with the treated DNA. Fusidic acid-resistant mutants isolated in this way have been shown to be predominantly of the low efficiency class. We have previously reported that most mutations of spontaneous origin occurring in this locus are of the high efficiency class, and have suggested that discrimination results from the elimination of specific classes of base pair mismatches that occur as intermediates in transformation. It would appear that the base pair mismatches most effectively eliminated in the discriminating strain of pneumococcus are those of the A:C and G:T type and that the immediate product of transformation with mutagenized DNA involves intermediates that are not recognized as A:C or G:T by the discrimination system.

Base Sequence↗
PubMed1986

Antigiardial activity of the bile salt-like antibiotic sodium fusidate.

Possible antigiardial activity of the bile salt-like antibiotic, sodium fusidate has been investigated during 24 h liquid culture of Giardia lamblia trophozoites and in 4 h microassays for parasite motility inhibition and viability. Sodium fusidate inhibited Giardia growth (ED50 0.2 mM; MIC 0.3 mM) but was considerably less potent than metronidazole (ED50 0.002 mM; MIC 0.05 mM). Sodium fusidate and metronidazole were active inhibitors of parasite motility (ED50 0.9 and 0.3 mM respectively) but were largely without effect in the 4 h viability assay. Sodium fusidate was active at concentrations well below its critical micellar concentration (2.7 mM) suggesting that its effect was not merely related to its membranolytic detergent properties. Its taurine and glycine conjugates were markedly less potent and paradoxically stimulated growth at low concentration. The studies suggest that sodium fusidate does have antigiardial activity and in view of its relative freedom from teratogenic and other toxic effects may be useful in pregnancy when other antigiardial agents are contra-indicated or as an adjunct in combination therapy when other single agents have failed to eradicate infection.

Animals↗
PubMed2000

Domain III of elongation factor G from Thermus thermophilus is essential for induction of GTP hydrolysis on the ribosome.

Two elongation factors (EF) EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. In the present paper we report that: (a) intrinsic GTPase activity of EF-G is influenced by excision of its domain III; (b) the EF-G lacking domain III has a 10(3)-fold decreased GTPase activity on the ribosome, whereas its affinity for GTP is slightly decreased; and (c) the truncated EF-G does not stimulate translocation despite the physical presence of domain IV, which is also very important for translocation. By contrast, the interactions of the truncated factor with GDP and fusidic acid-dependent binding of EF-G.GDP complex to the ribosome are not influenced. These findings indicate an essential contribution of domain III to activation of GTP hydrolysis. These results also suggest conformational changes of the EF-G molecule in the course of its interaction with the ribosome that might be induced by GTP binding and hydrolysis.

Bacterial Proteins↗