Literature DB >> 6762127

Serological approaches for the characterization of catalase in tissue-derived mycobacteria.

V M Katoch, L G Wayne, G A Diaz.   

Abstract

Cell-free extracts of Mycobacterium lepraemurium from mouse liver and M. leprae from armadillo liver were analysed for the presence of any mycobacterial catalase by using the specific inhibitor 3-amino-1,2,4-triazole and seroprecipitation titrations. These studies clearly demonstrated the presence of a "T" type of mycobacterial catalase in M. lepraemurium and placed it, in terms of immunological distance, in a position between M. tuberculosis and M. avium. The results did not reveal any detectable "T" catalase activity 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 bound to the extent of 80% to antisera against normal armadillo liver catalase. The significance of the component of the "M" catalase in M. leprae preparations which did not react against antibodies to normal liver remains to be determined.

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Year:  1982        PMID: 6762127

Source DB:  PubMed          Journal:  Ann Microbiol (Paris)        ISSN: 0300-5410


  3 in total

1.  Intrinsic catalase dot blot immunoassay for identification of Mycobacterium tuberculosis, Mycobacterium avium, and Mycobacterium intracellulare.

Authors:  L G Wayne; G A Diaz
Journal:  J Clin Microbiol       Date:  1987-09       Impact factor: 5.948

2.  Detection of a novel catalase in extracts of Mycobacterium avium and Mycobacterium intracellulare.

Authors:  L G Wayne; G A Diaz
Journal:  Infect Immun       Date:  1988-04       Impact factor: 3.441

3.  Catalases, peroxidases, and superoxide dismutases in Mycobacterium leprae and other mycobacteria studied by crossed immunoelectrophoresis and polyacrylamide gel electrophoresis.

Authors:  S T Lygren; O Closs; H Bercouvier; L G Wayne
Journal:  Infect Immun       Date:  1986-12       Impact factor: 3.441

  3 in total

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