Base de dados : HANSEN
Pesquisa : SUPEROXIDO DISMUTASE/METAB [Descritor de assunto]
Referências encontradas : 4 [refinar]
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Texto Completo-en
Id:27124
Autor:Marolia, Jolly; Mahadevan, PR.
Título:Reactive oxygen intermediates inactive Mycobacterium leprae in the phagocytes from human peripheral blood.
Fonte:Int J Lepr;57(2):483-491, June 1989. ^btab.
Resumo:Reactive oxygen intermediates such as hydrogen peroxide, superoxide, and hydroxyl radicals are important microbicidal components, and they could also play a role in an infection with Mycobacterium leprae. A comparative study of the level of hydrogen peroxide and superoxide produced by peripheral blood phagocytes from normal healthy individuals and lepromatous leprosy patients showed a deficiency in superoxide production in the patients. In the phagocytes from normal healthy individuals, there was good release of superoxide ions, and this mediated the killing of M. leprae. The lack of superoxide production allowed the viability of M. leprae inside the macrophages from leprosy patients. This deficiency could be rectified by the use of an immunomodulator, the delipidified cell wall of M. leprae. This modulation resulted in the ability of the patients' phagocytes to respond to M. leprae, to produce reactive oxygen intermediates such as superoxide, and also to kill the bacteria. These observations indicate that delipidified cell wall could have significant potential to positively modulate the immune-deficient cells of leprosy patients.^ien.
Descritores:Hanseníase Virchowiana/metab
Hanseníase Virchowiana/microbiol
Hanseníase Virchowiana/reabil
Mycobacterium leprae/imunol
Mycobacterium leprae/patogen
Superóxido Dismutase/bios
Superóxido Dismutase/metab
Meio Eletrônico:http://hansen.bvs.ilsl.br/textoc/revistas/intjlepr/1989/pdf/v57n2/v57n2a06.pdf - en.
Localização:Br191.1


  2 / 4 HANSEN  
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Id:17892
Autor:Wheeler, P. R; Gregory, D
Título:Superoxide dismutase, peroxidatic activity and catalase in Mycobacterium leprae purified from armadillo liver
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Fonte:s.l; s.n; dec. 1980. 8 p. graf.
Resumo:Superoxide dismutase has been identified and peroxidatic activity demonstrated in Mycobacterium leprae. The superoxide dismutase, shown indirectly to be a manganese-containing enzyme, was present at low activity in the cell-free extract. Peroxidatic activity was detected in a haemoprotein on polyacrylamide gels, but quantitative assay was not possible. Catalase, although present in a cell-free extract, appeared to be a host-derived enzyme, thus emphasizing the importance of establishing the authenticity of enzyme activities in host-derived M. leprae. The implications for the growth of M. leprae in vivo and its non-cultivability are discussed in the light of these findings.(AU).
Descritores:TATUS/metab
CATALASE/metab
FIGADO/enzimol
FIGADO/microbiol
MYCOBACTERIUM LEPRAE/enzimol
MYCOBACTERIUM LEPRAE/isol
PEROXIDOS/metab
SUPEROXIDO DISMUTASE/metab
HIDROXIDO DE SÓDIO/farmacol
Limites:ANIMAL
Meio Eletrônico: - .
Localização:BR191.1; 00755/s


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Id:15041
Autor:Mukhopadhyay, Asok; Panda, Amulya K; Pandey, Anil K
Título:Leprosy vaccine: influence of dissolved oxygen levels on growth of a candidate strain (mycobacterium w), and storage stability of the vaccine
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Fonte:s.l; s.n; 1998. 5 p. tab, graf.
Descritores:VACINAS BACTERIANAS
VACINAS BACTERIANAS
TÉCNICAS BACTERIOLOGICAS
CATALASE
ESTABILIDADE DE MEDICAMENTOS
ARMAZENAGEM DE MEDICAMENTOS
HANSENIASE
MYCOBACTERIUM
MYCOBACTERIUM
MYCOBACTERIUM
CONSUMO DE OXIGENIO
SUPEROXIDO DISMUTASE
BIORREATORES
Localização:BR191.1; 07280/s


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Id:13751
Autor:Deshpande, R. G; Khan, M. B; Bhat, D. A; Navalkar, R. G
Título:Superoxide dismutase activity of Mycobacterium tuberculosis isolated from tuberculosis patients and the immunoreactivity of superoxide dismutase from M. tuberculosis H37Rv
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Fonte:s.l; s.n; 1993. 7 p. ilus, tab.
Descritores:HANSENIASE
MYCOBACTERIUM TUBERCULOSIS
MYCOBACTERIUM TUBERCULOSIS
ANTICORPOS ANTIBACTÉRIAS
WESTERN BLOTTING
ELETROFORESE EM GEL DE POLIACRILAMIDA
ELISA
HIPERSENSIBILIDADE TARDIA
SUPEROXIDO DISMUTASE
SUPEROXIDO DISMUTASE
TUBERCULOSE PULMONAR
Limites:HUMANO
Localização:BR191.1; 06696/s



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