Superoxide dismutase, peroxidatic activity and catalase in Mycobacterium leprae purified from armadillo liver.
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.
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*
D010545:Peroxides; D012972:Sodium Hydroxide; D002374:Catalase; D013482:Superoxide Dismutase