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The Journal of Medical Microbiology, Vol 45, Issue 5 383-387, Copyright © 1996 by Society for General Microbiology

JOURNAL ARTICLE

Identification and characterisation of a superoxide dismutase and catalase from Mycobacterium ulcerans

B. Roberts and R. Hirst
Department of Biomedical and Tropical Veterinary Sciences, James Cook University of North Queensland, Townsville, Australia.

Previous investigations have demonstrated the presence of both superoxide dismutase and catalase enzymes in several intracellular pathogens, including a number of mycobacterial species. These enzymes are believed to be involved in the protection of the pathogen from the bactericidal products of oxidative metabolism. Superoxide dismutase and catalase were identified in crude extracts of Mycobacterium ulcerans by polyacrylamide gel electrophoresis. Inhibition experiments showed that the superoxide dismutase probably contained manganese as the metal cofactor. Other mycobacterial species examined for comparison produced bands of superoxide dismutase activity with a different mobility to that of M. ulcerans, suggesting possible structural differences between the enzymes.


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T.-J. KANG, J.-C. YOU, and G.-T. CHAE
Identification of catalase-like activity from Mycobacterium leprae and the relationship between catalase and isonicotinic acid hydrazide (INH)
J. Med. Microbiol., August 1, 2001; 50(8): 675 - 681.
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