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61.
Anne M. Berry Eric M. Glare David Hansman James C. Paton 《FEMS microbiology letters》1989,65(3):275-278
Twenty-four of 63 enteric Gram-negative organisms (38.1%) which were isolated from 35 apparently healthy Nigerian students were found to have low trimethoprim resistance (MIC less than 1000 mg/l). These isolates were also found to be resistant to several other antibiotics and trimethoprim resistance was found to be transferable from 15 (62.5%) of the trimethoprim resistant organisms into E. coli EC 1005. It is likely that the high percentage of trimethoprim resistance encountered in this study is related to the high rate of resistance transfer which was observed. 相似文献
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63.
Incubation of [14C] caffeine with hepatic microsomes from male AKR/J mice resulted in the formation of several metabolites including 1, 3, 7-trimethylurate and 6-amino-5-(N-formylmethyl-amino)-1, 3-dimethyluracil. These two compounds comprised about 60% of products and are major urinary metabolites in several animals. When cytosol was included during incubation, there was a 14-fold increase in yield of the uracil at the expense of the urate; the combination of the two metabolites remained about 60% of total products. Cytosol alone was catalytically inert. Glutathione and other sulfhydryl compounds reproduced the effect of cytosol, and the action of cytosol was accounted for quantitatively by its sulfhydryl content. We propose that an oxidized intermediate of caffeine en route to trimethylurate is reduced by glutathione to the ring-opened uracil derivative. 相似文献
64.
Mutations in Aprataxin cause the neurodegenerative syndrome ataxia oculomotor apraxia type 1. Aprataxin catalyzes removal of adenosine monophosphate (AMP) from the 5′ end of a DNA strand, which results from an aborted attempt to ligate a strand break containing a damaged end. To gain insight into which DNA lesions are substrates for Aprataxin action in vivo, we deleted the Saccharomyces cerevisiae HNT3 gene, which encodes the Aprataxin homolog, in combination with known DNA repair genes. While hnt3Δ single mutants were not sensitive to DNA damaging agents, loss of HNT3 caused synergistic sensitivity to H2O2 in backgrounds that accumulate strand breaks with blocked termini, including apn1Δ apn2Δ tpp1Δ and ntg1Δ ntg2Δ ogg1Δ. Loss of HNT3 in rad27Δ cells, which are deficient in long-patch base excision repair (LP-BER), resulted in synergistic sensitivity to H2O2 and MMS, indicating that Hnt3 and LP-BER provide parallel pathways for processing 5′ AMPs. Loss of HNT3 also increased the sister chromatid exchange frequency. Surprisingly, HNT3 deletion partially rescued H2O2 sensitivity in recombination-deficient rad51Δ and rad52Δ cells, suggesting that Hnt3 promotes formation of a repair intermediate that is resolved by recombination. 相似文献
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66.
Michitaro Nagasawa James Amigo Chan Charles J. Sih 《Prostaglandins & other lipid mediators》1974,8(3):221-230
Prostaglandins E1, F1α and A2 were covalently joined to the surface of Sepharose as carboxamide linkages. The insolubilized prostaglandins were shown to function effectively in the purification of 15(S) -hydroxyprostaglandin dehydrogenase. 相似文献
67.
Serotyping is the foundation of pathogenic Escherichia coli diagnostics; however, few laboratories have this capacity. We developed a molecular serotyping protocol that targets, genetically, the same somatic and flagellar antigens of E. coli O26:H11 used in traditional serotyping. It correctly serotypes strains untypeable by traditional methods, affording primary laboratories serotyping capabilities. 相似文献
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70.
E. coli cells containing a temperature-sensitivednaE mutation, in the α-subunit of holoenzyme DNA polymerase III, do not survive at the restrictive temperature. Such cells may
survive in the presence of thepcbA1 mutation, an allele of thegyrB gene. Such survival is dependent on an active DNA polymerase I. Evidence indicates that DNA polymerase I interacts directly
in the replisome (REP·A). Despite normal survival for cells using thepcbA replication pathway after some type of DNA damage, we have noted a failure of damage-induced mutagenesis. Here we present
evidence supporting a model of replisome pausing in cells dependent upon thepcbA replication pathway. The model argues that the (REP·A) complex pauses longer at the site of the lesion, allowing excision
repair to occur completely. In the normal replication pathway (REP·E) bypass of the lesion occurs, fixing the mutation. 相似文献