1887

INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY logo

Volume 32, Issue 3

Serological, Taxonomic, and Kinetic Studies of the T and M Classes of Mycobacterial Catalase Free

Abstract

Two types of catalase may be found in extracts of mycobacteria, the heat-labile T class and the heat-stable M class. The T-catalase is resistant to 3-amino-1,2,4-triazole and has a Michaelis constant in the range of 3.1 to 6.8 mM HO, whereas the M-catalase is inhibited by 3-amino-1,2,4-triazole and has a Michaelis constant in the range of 143 to 156 mM. Some species of mycobacteria produce only one class of catalase, and others produce both. Of the species studied, only , and . failed to exhibit T-catalase, although all three of these species had M-catalase. Conversely, . , . , . , , ., . , and . yielded T-catalase but not M-catalase. Six species, . ,. , . , . ,. , and . , produced both classes. The differences in resistance to heat and 3-amino-1,2,4-triazole were exploited in the development of methods for quantitative serological characterization of one class of catalase in the presence of the other. These techniques were used with three reference sera to produce a branching diagram of divergence of the T-catalases from 13 species of mycobacteria based on measurements of immunological distance. No T-catalase could be demonstrated in another three species. A first-stage study was also carried out with a single reference antiserum to M-catalase from . . Representatives of nine mycobacterial species, including the three that produced no T-catalase, were characterized with this reference system, which tends to yield larger immunological distance values than the T-catalase system.

  • Published Online:
Copyright © 1982 International Union of Microbiological Societies
Loading

Article metrics loading...

/content/journal/ijsem/10.1099/00207713-32-3-296
1982-07-01
2024-04-24
Loading full text...

Full text loading...

/deliver/fulltext/ijsem/32/3/ijs-32-3-296.html?itemId=/content/journal/ijsem/10.1099/00207713-32-3-296&mimeType=html&fmt=ahah

References

  1. Aebi H. 1974; Catalase. 673–684 Bergmeyer H. U. Methods of enzymatic analysis, 2. Academic Press, Inc.; New York:
     [Google Scholar]
  2. Andrejew A., Gemez-Rieux C. 1962; Essais de differenciation des mycobacteries d’apres la sensibilite de leur activite catalasique aux inhibiteurs. Ann. Inst. Pasteur Paris 103:201–215
     [Google Scholar]
  3. Bartholomew R. 1968; Multiple catalase enzymes in two species of mycobacteria. Am. Rev. Respir. Dis 97:710–712
     [Google Scholar]
  4. Claiborne A., Fridovich I. 1979; Purification of the o-dianisidine peroxidase from Escherichia coli B. Physico-chemical characterization and analysis of its dual catalatic and peroxidatic activities. J. Biol. Chem 254:4245–4252
     [Google Scholar]
  5. Cocks G. T., Wilson A. C. 1972; Enzyme evolution in the Enterobacteriaceae. . J. Bacteriol 110:793–802
     [Google Scholar]
  6. Devi B. G., Shaila M. S., Ramakrishnan L., Gopinathan K. P. 1975; The purification and properties of peroxidase in M.tuberculosis H37Rv and its possible role in the mechanism of action of isonicotinic acid hydrazide. J. Biochem. (Tokyo) 149:187–197
     [Google Scholar]
  7. Diaz G. A., Wayne L. G. 1974; Isolation and characterization of catalase produced by M. tuberculosis. . Am. Rev. Respir. Dis 110:312–319
     [Google Scholar]
  8. Hassan H., Fridovich I. 1979; Superoxide, hydrogen peroxide, and oxygen tolerance of oxygen-sensitive mutants of Escherichia coli . Rev. Infect. Dis 1:357–367
     [Google Scholar]
  9. Kubica G. P., Pool G. L. 1960; Studies on catalase activity of acid-fast bacilli. Am. Rev. Respir. Dis 81:387–391
     [Google Scholar]
  10. Norgard M., Imaeda T. 1980; Heterogeneity of deoxyribonucleic acid molecules isolated from Mycobacterium smegmatis . J. Bacteriol 144:766–771
     [Google Scholar]
  11. Prager E. M., Wilson A. C. 1971; The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. J. Biol. Chem 246:5978–5989
     [Google Scholar]
  12. Schleifer K.-H., Meyer S. A., Rupprecht M. 1979; Relatedness among coagulase-negative staphylococci: de-oxyribonucleic acid reassociation and comparative immunological studies. Arch. Microbiol 122:93–101
     [Google Scholar]
  13. Schweiger O., Roman E., Soos I. 1958; Studies on the catalase enzyme of mycobacteria. I. Correlation between catalase activity and virulence of mycobacteria under certain experimental conditions. Am. Rev. Respir. Dis 77:146–154
     [Google Scholar]
  14. Wayne L. G., Diaz G. A. 1976; Immunoprecipitation studies of mycobacterial catalase. Int. J. Syst. Bacteriol 26:38–44
     [Google Scholar]
  15. Wayne L. G-, Diaz G. A. 1979; Reciprocal immunological distances of catalase derived from strains of My cobacterium avium Mycobacterium tuberculosis, and closely related specie. Int. J. Syst. Bacteriol 29:19–24
     [Google Scholar]
  16. Wayne L. G., Diaz G. A., Doubek J. R. 1968; Acquired isoniazid resistance and catalase activity. Am. Rev. Respir. Dis 97:909–913
     [Google Scholar]
  17. Wolinsky E. 1979; Nontuberculous mycobacteria and associated diseases. Am. Rev. Respir. Dis 119:107–159
     [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/ijsem/10.1099/00207713-32-3-296
Loading
Serological, Taxonomic, and Kinetic Studies of the T and M Classes of Mycobacterial Catalase
Int J Syst Evol Microbiol 32, 296 (1982); https://doi.org/10.1099/00207713-32-3-296
/content/journal/ijsem/10.1099/00207713-32-3-296
/content/journal/ijsem/10.1099/00207713-32-3-296
Loading

Data & Media loading...

Most cited Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error