Enzyme Electrophoretograms in the Analysis of Taxon Relatedness of and Atypical Neisserias Free

Abstract

SUMMARY: Extracts were prepared from several strains of and spp. Esterases, NADP-dependent isocitrate dehydrogenase and malate dehydrogenase activities were assayed after electrophoresis of extracts of polyacrylamide gels. Except for and which resolved activity bands for the acetate-esterase only, the remaining bacteria exhibited species-specific esterase patterns also for the propionate and butyrate substrates. The multiple esterase patterns from 25238 were qualitatively and quantitatively different from those of 23246. This finding and other evidence supports a taxonomic shift of the latter to a species level of that genus. The atypical neisserias and appeared to exhibit an intrageneric specificity in their esterase patterns with those from but not to the other spp. tested. The malate dehydrogenase patterns from the atypical neisserias and 23246 were qualitatively similar; however, the patterns of isocitrate dehydrogenase activity were variable for these species. was distinct in its esterase and dehydrogenase bands, strongly suggesting its taxon unrelatedness to the genus or the atypical neisserias. Of the enzymes assayed, esterase proved to be the most reliable for taxonomic identifications.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-86-2-210
1975-02-01
2024-03-29
Loading full text...

Full text loading...

/deliver/fulltext/micro/86/2/mic-86-2-210.html?itemId=/content/journal/micro/10.1099/00221287-86-2-210&mimeType=html&fmt=ahah

References

  1. Baumann P., Doudoroff M., Stanier R. Y. 1968; Study of the Moraxella group. I. Genus Moraxella and the Neisseria catarrhalis group. Journal of Bacteriology 95:58–73
    [Google Scholar]
  2. Boháček J., Kocur M., Martinec T. 1969; DNA base composition and taxonomy of some micrococci. Journal of General Microbiology 46:369–376
    [Google Scholar]
  3. Bøvre K. 1967; Transformation and DNA base composition in taxonomy with special reference to recent studies in Moraxella and Neisseria. Acta pathologica et microbiologica scandinavica 69:123–144
    [Google Scholar]
  4. Bøvre K., Fiandt M., Szybalski W. 1967; DNA base composition of Neisseria, Moraxella and Acinetobacter, as determined by measurements of buoyant density of CsCl gradients. Canadian Journal of Microbiology 15:335–338
    [Google Scholar]
  5. Catlin B. W. 1970; Transfer of the organism named Neisseria catarrhalis to Branhamella gen. nov. International Journal of Systematic Bacteriology 20:155–159
    [Google Scholar]
  6. Catlin B. W., Cunningham L. S. 1961; Transforming activities and base contents of deoxyribonucleate preparations from various neisseriae. Journal of General Microbiology 26:303–312
    [Google Scholar]
  7. Catlin B. W., Cunningham L. S. 1964; Genetic transformation of Neisseria catarrhalis by deoxyribonucleate preparations having different average base compositions. Journal of General Microbiology 37:341–352
    [Google Scholar]
  8. El-Sharkawy T. A., Huisingh D. 1971a; Electrophoretic analysis of esterases and other soluble proteins from representatives of phytopathogenic bacterial genera. Journal of General Microbiology 68:149–154
    [Google Scholar]
  9. El-Sharkawy T. A., Huisingh D. 1971b; Differentiation among Xanthomonas species by polyacryl-amide gel electrophoresis of soluble proteins. Journal of General Microbiology 68:155–165
    [Google Scholar]
  10. Fox R. H., Mcclain D. E. 1974; Evaluation of the taxonomic relationship of Micrococcus cryophilus, Branhamella catarrhalis and Neisseriae by comparative polyacrylamide gel electrophoresis of soluble proteins. International Journal of Systematic Bacteriology 24:172–176
    [Google Scholar]
  11. Henriksen S. D., Bøvre K. 1968; The taxonomy of the genera Moraxella and Neisseria. Journal of General Microbiology 51:387–392
    [Google Scholar]
  12. Kingsbury D. T. 1967; Deoxyribonucleic acid homologies among species of the genus Neisseria. Journal of Bacteriology 94:870–874
    [Google Scholar]
  13. Lamacchia E. H., Pelczar J. J. 1966; Analyses of deoxyribonucleic acid of Neisseria caviae and other Neisseria. Journal of Bacteriology 91:514–516
    [Google Scholar]
  14. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  15. Lund B. M. 1965; A comparison by the use of gel electrophoresis of soluble protein components and esterase enzymes of some group D streptococci. Journal of General Microbiology 40:413–419
    [Google Scholar]
  16. Mazenec K., Kocur M., Martinec T. 1966; Electron microscopy of ultra-thin sections of Micrococcus cryophilus. Canadian Journal of Microbiology 12:465–469
    [Google Scholar]
  17. Ochoa S. 1955; Malic dehydrogenase from pig heart. In Methods in Enzymology 1 pp. 735–736 Colwick S. P., Kaplan N. O. Edited by New York: Academic Press;
    [Google Scholar]
  18. Robinson K. 1966; An examination of Corynebacterium spp. by gel electrophoresis. Journal of Applied Bacteriology 29:179–184
    [Google Scholar]
  19. Rowe J. J., Reeves H. C. 1971; Electrophoretic heterogeneity of bacterial nicotinamide adenine dinucleotide phosphate-specific isocitrate dehydrogenase. Journal of Bacteriology 108:824–827
    [Google Scholar]
  20. Sleytr U., Kocur M. 1971; Structure of Micrococcus cryophilus after freeze-etching. Archiv für Mikrobiologie 78:353–359
    [Google Scholar]
  21. Thomas A. D., Doelle H. W., Westwood A. W., Gordon G. L. 1972; Effect of oxygen on several enzymes involved in the aerobic and anaerobic utilization of glucose in Escherichia coli. Journal of Bacteriology 112:1099–1105
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-86-2-210
Loading
/content/journal/micro/10.1099/00221287-86-2-210
Loading

Data & Media loading...

Most cited Most Cited RSS feed