Superoxide Dismutase, Peroxidatic Activity and Catalase in Mycobacterium leprae Purified from Armadillo Liver

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Abstract
Superoxide dismutase (EC 1.15.1.1) was identified and peroxidatic activity demonstrated in M. leprae. The superoxide dismutase, shown indirectly to be a Mn-containing enzyme, was present at low activity in the cell-free extract. Peroxidatic activity was detected in a hemoprotein on polyacrylamide gels, but quantitative assay was not possible. Catalse (EC 1.11.1.6) was present in a cell-free extract but appeared to be a host-derived enzyme, 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 noncultivability are discussed. [M. leprae was isolated from the livers of heavily infected armadillos, Dasypus movemcinctus.].

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