@article{mbs:/content/journal/micro/10.1099/00221287-121-2-457, author = "Wheeler, P. R. and Gregory, D.", title = "Superoxide Dismutase, Peroxidatic Activity and Catalase in Mycobacterium leprae Purified from Armadillo Liver", journal= "Microbiology", year = "1980", volume = "121", number = "2", pages = "457-464", doi = "https://doi.org/10.1099/00221287-121-2-457", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-121-2-457", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", 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.", }