SEROLOGICAL APPROACHES FOR THE CHARACTERIZATION OF CATALASE IN TISSUE-DERIVED MYCOBACTERIA
- 1 January 1982
- journal article
- research article
- Vol. B133 (3) , 407-414
Abstract
Cell-free extracts of Mycobacterium lepraemurium from mouse liver and M. leprae from armadillo liver were analyzed for the presence of mycobacterial catalase by using the specific inhibitor 3-amino-1,2,4-triazole and seroprecipitation titrations. The presence of a T type mycobacterial catalase was demonstrated in M. lepraemurium, placing it, in terms of immunological distance, between M. tuberculosis and M. avium. No T catalase activity was revealed in the M. leprae preparations. The M type catalase activity which was observed did not bind to antisera against M catalase of M. kansasii, but was 80% bound to antisera against normal armadillo liver catalase. The significance of the component of the M catalase in M. leprae preparations which do not react with antibodies to normal liver catalase remains to be determined.This publication has 1 reference indexed in Scilit:
- Reciprocal Immunological Distances of Catalase Derived from Strains of Mycobacterium avium, Mycobacterium tuberculosis, and Closely Related SpeciesInternational Journal of Systematic and Evolutionary Microbiology, 1979