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Id:17919
Autor:Rasbridge, Marian M; Scott, G. L
Título:The haemolytic action of dapsone: changes in the red-cell membrane
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Fonte:s.l; s.n; feb. 1973. 11 p. tab, graf.
Resumo:Some aspects of red-cell membrane structure and function have been investigated in patients with haemolysis due to dapsone (4,4' diaminodiphenylsulfone). Osmotic fragility and potassium flux were not increased but red-cell membrane changes occurred which suggest instability. These included loss of phospholipid, decrease in acetylcholinesterase activity and increased autohaemolysis. In addition, there was evidence for lipid peroxidation, which might have been the primary lesion. Red-cell membrane sulphydryl group activity was either reduced or altered because these cells were abnormally sensivite to the action of the sulphydryl group inhibitor p-chloromercuribenzoate, as measured by increased potassium leakage and haemolysis. Dapsone also caused abnormal peroxide lysis in the presence of normal hydrogen peroxide detoxification mechanisms and in the absence of vitamin E deficiency. This was prevented by excess vitamin E but not by the sulphydryl compounds, reduced glutathione or cysteine, and it was increased by previous treatment with p-chloromercuribenzoate. It is suggested that the reduced membrane sulphydryl group activity, probably due to the formation of mixed disulphides with precipitated haemoglobin, and lipid proxidation may be responsible for in vitro and, possibly, in vivo dapsone-induced haemolysis.(AU).
Descritores:ACETILCOLINESTERASE/sangue
MEMBRANA CELULAR/ef drogas
DAPSONA/ef adv
DERMATITE HERPETIFORME/quimioter
HEMOLISE/ef drogas
LIPIDIOS/metab
FRAGILIDADE OSMOTICA
PEROXIDOS/metab
FOSFOLIPIDIOS/sangue
COMPOSTOS DE SULFIDRILA
Limites:MASCULINO
FEMININO
MEIA-IDADE
Meio Eletrônico: - .
Localização:BR191.1; 01857/s


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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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