title: Superoxide dismutase, peroxidatic activity and catalase in Mycobacterium leprae purified from armadillo liver.
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.
mesh_terms: D000818:Animals; D001135:Armadillos / Q000378:metabolism; D002374:Catalase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology / Q000382:microbiology; D009166:Mycobacterium leprae / Q000201:enzymology* / Q000302:isolation & purification; D010545:Peroxides / Q000378:metabolism*; D012972:Sodium Hydroxide / Q000494:pharmacology; D013482:Superoxide Dismutase / Q000378:metabolism*
chemical_list: D010545:Peroxides; D012972:Sodium Hydroxide; D002374:Catalase; D013482:Superoxide Dismutase