RESUMO
OBJECTIVES: The aim of this study was to determine the amount of magnesium sulfate involved when we diagnose a severe preeclampsia in pregnant women. Other goals were to know what the MgSO4 side-effects and complications are, and what benefits this treatment brings to prevent an eclampsia. PATIENTS AND METHODS: This retrospective and descriptive study was conducted for 7 years. We identified 105 women treated by MgSO4 out of 560 preeclampsia cases. To prevent eclampsia, those women were administrated MgSO4 before, during or after labor. All data about hospitalization term and MgSO4 term administration were collected in order to understand if MgSO4 side-effects for the women and the fetus occurred before, during or after labor. Those tables are compared with the MgSO4 administered dosages. RESULTS: MgSO4 isn't systematically used in all the preeclampsia cases. Forty percent of women under treatment presented low side effects. Overdoses, encountered in 31.4% of cases, regressed as soon as the MgSO4's perfusion was stopped. No major complications were noted. Only 0.95% of women treated by MgSO4 presented an eclampsia. DISCUSSION AND CONCLUSION: MgSO4 administered only to women having a neurological preeclampsia, within therapeutic doses and with rigorous monitoring, does not bring deleterious effects to the mother or newborn baby. Consequently, MgSO4's benefits were above the risks.
Assuntos
Sulfato de Magnésio/administração & dosagem , Pré-Eclâmpsia/tratamento farmacológico , Relação Dose-Resposta a Droga , Eclampsia/prevenção & controle , Feminino , Humanos , Recém-Nascido , Sulfato de Magnésio/efeitos adversos , Pré-Eclâmpsia/diagnóstico , Gravidez , Estudos RetrospectivosRESUMO
Two NADPH-dependent disulfide reductases, glutathione reductase and trypanothione reductase, were shown to be present in Euglena gracilis, purified to homogeneity and characterized. The glutathione reductase (Mr 50 kDa) displays a high specificity towards glutathione disulfide with a KM of 54 microM. The amino acid sequences of two peptides derived from the trypanothione reductase (Mr 54 kDa) show a high level of identity (81% and 64%) with sequences of trypanothione reductases from trypanosomatids. The trypanothione reductase is able to efficiently reduce trypanothione disulfide (KM 30.5 microM) and glutathionylspermidine disulfide (KM 90.6 microM) but not glutathione disulfide, nor Escherichia coli thioredoxin disulfide, nor 5,5'-dithiobis(2-nitrobenzoate) (DTNB). These results demonstrate for the first time (i) the existence of trypanothione reductase in a non-trypanosomatid organism and (ii) the coexistence of trypanothione reductase and glutathione reductase in E. gracilis.