RESUMO
In this paper, the performance of a previously developed classification system applied to pharmaceutical chromatographic analyses, is investigated. The separation of seven different drug substances from their respective impurities was studied. The chromatographic procedure for acetylsalicylic acid, clindamycin hydrochloride, buflomedil hydrochloride, chloramphenicol sodium succinate, nimesulide and phenoxymethylpenicillin was performed according to the corresponding European Pharmacopoeia (Ph. Eur.) monograph. The separation of dihydrostreptomycin sulphate was performed according to the literature. It is shown that the column ranking system is a helpful tool in the selection of a suitable column in these analyses.
Assuntos
Cromatografia Líquida/instrumentação , Preparações Farmacêuticas/isolamento & purificação , Aspirina/isolamento & purificação , Cloranfenicol/análogos & derivados , Cloranfenicol/isolamento & purificação , Cromatografia Líquida/métodos , Clindamicina/isolamento & purificação , Sulfato de Di-Hidroestreptomicina/isolamento & purificação , Penicilina V/isolamento & purificação , Pirrolidinas/isolamento & purificação , Sensibilidade e Especificidade , Sulfonamidas/isolamento & purificaçãoAssuntos
Antibacterianos/isolamento & purificação , Sulfato de Di-Hidroestreptomicina/análogos & derivados , Streptomyces/metabolismo , Antibacterianos/farmacologia , Fenômenos Químicos , Química , Sulfato de Di-Hidroestreptomicina/isolamento & purificação , Sulfato de Di-Hidroestreptomicina/farmacologia , Espectroscopia de Ressonância MagnéticaRESUMO
Accumulation of purified adenylylated dihydrostreptomycin (DHS-AMP) was examined in two strains of Escherichia coli. E. coli JSRO-N was plasmid free and aminoglycoside (AG) susceptible; E. coli JSRO-N(pSAD1) contained a plasmid-encoded AG adenylyltransferase which modifies DHS and streptomycin and confers resistance to both of these drugs. Although both whole cells and spheroplasts of JSRO-N accumulated free DHS, we were not able to demonstrate uptake of DHS-AMP by this strain. Whole cells and spheroplasts of JSRO-N(pSAD1) accumulated DHS at a much slower rate than that observed in JSRO-N. This was presumably due to the activity of the adenylyltransferase in JSRO-N(pSAD1). However, this low rate of accumulation of DHS was still higher than the uptake of DHS-AMP by either JSRO-N or JSRO-N(pSAD1). Thus, the rate of accumulation of DHS-AMP was even lower than that of DHS during the slow, initial, energy-dependent phase of AG uptake seen in JSRO-N(pSAD1). We also found that when either JSRO-N or JSRO-N(pSAD1) was incubated with barely inhibitory or subinhibitory concentrations of DHS, rapid uptake of DHS could be stimulated by the addition of an inhibitory concentration of another AG, such as amikacin. Uptake of DHS-AMP could not be similarly enhanced by the addition of amikacin. Our results indicate that DHS-AMP is not accumulated by whole cells or spheroplasts of E. coli. These results are consistent with the postulated intracellular location of AG-modifying enzymes.
