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At least 973 records · Page 54Linked to original sources
PubMed1984

Cysticercosis.

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Cysticercosis↗
PubMed1961

Excretion of antibiotics in bile.

The excretion of antibiotics in the bile of rats has been studied. Penicillins, including derivatives of 6-aminopenicillanic acid, are rapidly excreted, reabsorbed and re-excreted, in high concentration, whereas streptomycin, neomycin, paramomycin and chloramphenicol reach lower levels in the bile than in the plasma. p-Aminobenzylpenicillin and D(-)-6-(alpha-amino-alpha-phenylacetamido)penicillanic acid, both of which are bactericidal to Salmonellae and other coliforms, produce higher concentrations in the bile than benzylpenicillin (penicillin G). This may be of therapeutic importance.

Ampicillin↗
PubMed1967

Phenotype masking and streptomycin dependence.

In attempting to define the role of ribosomes in the mechanism of streptomycin dependence, a new phenomenon has been discovered. Analysis of this phenomenon-called phenotypic masking-leads to the conclusion that "streptomycin dependent" mutants are actually "drug dependent" because their dependence is equally satisfied by several drugs. These drugs, some of which are totally unrelated chemically, act on the ribosome and induce misreading in vitro and suppression in vivo.

Drug Resistance, Microbial↗
PubMed1999

Recognition of the codon-anticodon helix by ribosomal RNA.

Translational fidelity is established by ribosomal recognition of the codon-anticodon interaction within the aminoacyl-transfer RNA (tRNA) site (A site) of the ribosome. Experiments are presented that reveal possible contacts between 16S ribosomal RNA and the codon-anticodon complex. N1 methylation of adenine at position 1492 (A1492) and A1493 interfered with A-site tRNA binding. Mutation of A1492 and A1493 to guanine or cytosine also impaired A-site tRNA binding. The deleterious effects of A1492G or A1493G (or both) mutations were compensated by 2'fluorine substitutions in the mRNA codon. The results suggest that the ribosome recognizes the codon-anticodon complex by adenine contacts to the messenger RNA backbone and provide a mechanism for molecular discrimination of correct versus incorrect codon-anticodon pairs.

Adenine↗
PubMed1972

Activity of lividomycin against Pseudomonas aeruginosa: its inactivation by phosphorylation induced by resistant strains.

The antibacterial activity and enzymatic inactivation of lividomycin, a new aminoglycosidic antibiotic, were studied with 13 strains of Pseudomonas aeruginosa. The minimal inhibitory concentration of lividomycin was 12.5 to 25 mug/ml, and three strains were resistant to high concentrations of lividomycin (more than 200 mug/ml). It was found that P. aeruginosa TI-13 and K-11, highly lividomycin-resistant strains of clinical origin, strongly inactivated the drug. The third resistant strain, Km-41/R, was developed in vitro. Unlike the other resistant strains, Km-41/R, was developed in vitro. Unlike the other resistant strains, Km-41/R did not inactivate the drug, indicating that different mechanisms were involved in lividomycin resistance. By use of a cell-free extract from P. aeruginosa TI-13, the inactivation of lividomycin was found to be caused by the formation of a monophosphorylated product of the drug.

Drug Resistance, Microbial↗
PubMed1972

Antibacterial activity of lividomycin toward R factor-resistant strains of Escherichia coli.

Forty-eight R factors conferring resistance to both kanamycin (KM) and streptomycin (SM) were demonstrated from 1,270 Escherichia coli strains of clinical origin. Among these R factors isolated, 42 also conferred resistance to the new antibiotic lividomycin (LV). Extracts of E. coli ML1410 carrying one such factor (R(M81)) inactivated LV as well as KM and SM. But extracts of E. coli ML1410 carrying an R factor (R(M82) or R(M83)) sensitive to LV could not inactivate LV. LV inactivation required both adenosinetriphosphate (ATP) and Mg(2+). Inactivated LV was reactivable by alkaline phosphatase. Isotopic studies with labeled ATP and elemental analysis of the reaction product indicate that it is a monophosphorylated derivative of LV.

Drug Resistance, Microbial↗