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. 1988 Apr;56(4):936–941. doi: 10.1128/iai.56.4.936-941.1988

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

L G Wayne 1, G A Diaz 1
PMCID: PMC259394  PMID: 3346077

Abstract

A novel class of catalase, which differs from the previously described M- and T-catalases of mycobacteria, was detected in strains of Mycobacterium avium and M. intracellulare. Designated A-catalase, this enzyme resisted inactivation at 68 degrees C, was inactivated by 3-amino-1,2,4-triazole (aminotriazole), and exhibited no peroxidase activity. All of these properties distinguished the enzyme from T-catalase. The A-catalase exhibited a Km of 70 mM H2O2, which is between the upper and lower extremes of the ranges reported for T- and M-catalases, respectively. The A-catalase appeared to be more hydrophobic than M-catalase and did not react with antiserum to a representative sample of this class. The banding patterns of T- and M-catalases seen by polyacrylamide gel electrophoresis (PAGE) were essentially unaffected by the incorporation of sodium dodecyl sulfate (SDS) into the PAGE system, whereas the single band of A-catalase seen by PAGE without SDS resolved into as many as five bands in the presence of SDS; these bands were all of slower mobility than the original band. The banding pattern seen with SDS appeared to be related more to counterion charge effects than to molecular size increases that could be attributed to SDS complexed to the protein. It remains to be determined whether the multiple A-catalase bands reflect different proteins or different SDS micellar complexes of a single protein.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Claiborne A., Fridovich I. Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities. J Biol Chem. 1979 May 25;254(10):4245–4252. [PubMed] [Google Scholar]
  2. Jones M. N., Manley P., Midgley P. J., Wilkinson A. E. Dissociation of bovine and bacterial catalases by sodium n-dodecyl sulfate. Biopolymers. 1982 Jul;21(7):1435–1450. doi: 10.1002/bip.360210712. [DOI] [PubMed] [Google Scholar]
  3. KUBICA G. P., POOL G. L. Studies on the catalase activity of acid-fast bacilli. I. An attempt to subgroup these organisms on the basis of their catalase activities at different temperatures and pH. Am Rev Respir Dis. 1960 Mar;81:387–391. doi: 10.1164/arrd.1960.81.3.387. [DOI] [PubMed] [Google Scholar]
  4. Katoch V. M., Wayne L. G., Diaz G. A. Serological approaches for the characterization of catalase in tissue-derived mycobacteria. Ann Microbiol (Paris) 1982 Nov-Dec;133(3):407–414. [PubMed] [Google Scholar]
  5. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  6. Lygren S. T., Closs O., Bercouvier H., Wayne L. G. Catalases, peroxidases, and superoxide dismutases in Mycobacterium leprae and other mycobacteria studied by crossed immunoelectrophoresis and polyacrylamide gel electrophoresis. Infect Immun. 1986 Dec;54(3):666–672. doi: 10.1128/iai.54.3.666-672.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Shoeb H. A., Bowman B. U., Jr, Ottolenghi A. C., Merola A. J. Evidence for the generation of active oxygen by isoniazid treatment of extracts of Mycobacterium tuberculosis H37Ra. Antimicrob Agents Chemother. 1985 Mar;27(3):404–407. doi: 10.1128/aac.27.3.404. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Shoeb H. A., Bowman B. U., Jr, Ottolenghi A. C., Merola A. J. Peroxidase-mediated oxidation of isoniazid. Antimicrob Agents Chemother. 1985 Mar;27(3):399–403. doi: 10.1128/aac.27.3.399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Wayne L. G., Diaz G. A. A double staining method for differentiating between two classes of mycobacterial catalase in polyacrylamide electrophoresis gels. Anal Biochem. 1986 Aug 15;157(1):89–92. doi: 10.1016/0003-2697(86)90200-9. [DOI] [PubMed] [Google Scholar]
  10. Wayne L. G., Diaz G. A. Identification of mycobacteria by specific precipitation of catalase with absorbed sera. J Clin Microbiol. 1985 May;21(5):721–725. doi: 10.1128/jcm.21.5.721-725.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Wayne L. G., Diaz G. A. Intrinsic catalase dot blot immunoassay for identification of Mycobacterium tuberculosis, Mycobacterium avium, and Mycobacterium intracellulare. J Clin Microbiol. 1987 Sep;25(9):1687–1690. doi: 10.1128/jcm.25.9.1687-1690.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Wayne L. G., Krichevsky M. I., Portyrata D., Jackson C. K. Diagnostic probability matrix for identification of slowly growing mycobacteria in clinical laboratories. J Clin Microbiol. 1984 Oct;20(4):722–729. doi: 10.1128/jcm.20.4.722-729.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Wheeler P. R., Gregory D. Superoxide dismutase, peroxidatic activity and catalase in Mycobacterium leprae purified from armadillo liver. J Gen Microbiol. 1980 Dec;121(2):457–464. doi: 10.1099/00221287-121-2-457. [DOI] [PubMed] [Google Scholar]

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