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J. Biochem, 1977, Vol. 81, No. 5 1427-1433
© 1977 Japanese Biochemical Society

research-article

Superoxide Dismutase from Mycobacterium lepraemurium

Kosuke ICHIHARA1,*, Emi KUSUNOSE*, Masamichi KUSUNOSE2,* and Tatsuo MORI**

*Toneyama Institute for Tuberculosis Research, Osaka City University Medical School Toyonaka, Osaka 560
**Department of Leprology, Research Institute for Microbial Diseases, Osaka University Suita, Osaka 564

2Communications should be addressed to: M. Kusunose, Toneyama Institute for Tuberculosis Research, Toneyama 5-1-I, Toyonaka 560

Mycobacterium lepraemurium, strain Hawaii, grown on 1% Ogawa egg yolk medium containing hemin, was extremely rich in superoxide dismutase [EC 1.15.1.1 [EC] ]. This enzyme accounted for at least 7% of total proteins in the crude extracts, as determined by immunological procedures. The enzyme was purified about 18.5-fold from the crude extracts by streptomycin treatment, ammonium sulfate fractionation, and Sephadex G-100 gel filtration. The homogeneity of the purified enzyme was established by polyacrylamide gel electrophoresis, analytical ultracentrifugation, and irnmunodiffusion. The molecular weight of the enzyme was estimated to be approximately 45,000 by sedimentation equilibrium analysis, whereas that of the subunit was 22,000 as determined by sodium dodecylsulfate-polyacrylamide gel electrophoresis. The enzyme was found to contain 1.29 g atom of manganese per mol by atomic absorption spectroscopy. In addition, a small but significant amount of iron was found. The amino acid composition was similar to that of the superoxide dismutase from Mycobacterium smegmatis. Superoxide dismutase is the first enzyme which has been isolated and characterized from M. lepraemurium.

1Present address Department of Biochemistry, Kawasaki Medical School, Kurashiki 701-01.


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