RESUMO
We herein report a clinical pitfall regarding the treatment of a case of pulmonary tuberculoma in a patient with chronic hepatitis C. The patient presented with both chronic hepatitis C and pulmonary tuberculoma, and we initiated treatment of the chronic hepatitis C first due to the potential for liver injury; however, the patient's condition worsened in terms of the pulmonary tuberculosis. This case highlights the need to select the initial treatment for pulmonary tuberculoma, not chronic hepatitis C. In addition, we report that, although the administration of anti-tuberculosis chemotherapy regimens containing pyrazinamide (PZA) substantially increases the incidence of drug-induced hepatitis in patients with chronic hepatitis, we were fortunately able to use PZA without observing drug-induced hepatitis in this case because we closely monitored the patient's liver function.
Assuntos
Antituberculosos/uso terapêutico , Antivirais/uso terapêutico , Hepatite C Crônica/tratamento farmacológico , Tuberculoma/tratamento farmacológico , Tuberculose Pulmonar/tratamento farmacológico , DNA Viral/análise , Quimioterapia Combinada , Feminino , Seguimentos , Hepacivirus/genética , Hepatite C Crônica/complicações , Humanos , Biópsia Guiada por Imagem , Isoniazida/uso terapêutico , Pulmão/diagnóstico por imagem , Pulmão/microbiologia , Pulmão/patologia , Pessoa de Meia-Idade , Mycobacterium tuberculosis/isolamento & purificação , Guias de Prática Clínica como Assunto , Pirazinamida/uso terapêutico , Rifampina/uso terapêutico , Tomografia Computadorizada por Raios X , Tuberculoma/complicações , Tuberculoma/diagnóstico , Tuberculose Pulmonar/complicações , Tuberculose Pulmonar/diagnósticoRESUMO
Oxidative regeneration pathways of bovine pancreatic ribonuclease A (RNase A), which has four SS linkages, were studied at 25 degrees C and pH 8.0 by using trans-3,4-dihydroxy-1-selenolane oxide (DHS(ox)), a new selenoxide reagent with strong oxidation power. The short-term folding study using a quench-flow instrument ( approximately 1 min) revealed that early intermediates (1S, 2S, 3S and 4S) are formed stochastically and irreversibly from the reduced protein (R) and do not have any stable structures. In the long-term folding study ( approximately 300 min), on the other hand, slow generation of the key intermediates (des[65-72] and des[40-95]) through SS rearrangement from the 3S intermediate ensemble was observed, followed by slight formation of native RNase A (N). The parallel UV and CD measurements demonstrated that formation of the key intermediates is accompanied with the formation of the native-like structures. Thus, DHS(ox) allowed facile identification of the conformational folding steps coupled with SS rearrangement on the major oxidative folding pathways.
