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| Id: | 13259
| | Author: | Wheeler, P. R; Gregory, D
| | Title: | Superoxide dismutase, peroxidatic activity and catalase in Mycobacterium leprae purified from armadillo liver
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| | Source: | s.l; s.n; dec. 1980. 8 p. graf.
| | Abstract: | 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).
| | Descriptors: | TATUS/metab
CATALASE/metab
FIGADO/enzimol
FIGADO/microbiol
MYCOBACTERIUM LEPRAE/enzimol
MYCOBACTERIUM LEPRAE/isol
PEROXIDOS/metab
SUPEROXIDO DISMUTASE/metab
HIDROXIDO DE SÓDIO/farmacol
| | Limits: | ANIMAL
| | Electronic Medium: | http://www.ilsl.br
| | Location: | BR191.1; 00755/s |
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