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. 1963 Sep;86(3):585–592. doi: 10.1128/jb.86.3.585-592.1963

COMPLEMENTATION OF LECITHINASE ACTIVITIES BY CLOSELY RELATED PSEUDOMONADS: ITS TAXONOMIC IMPLICATION1

Janice L Bates a, Pinghui V Liu a
PMCID: PMC278477  PMID: 14066442

Abstract

Bates, Janice L. (University of Louisville School of Medicine, Louisville, Ky.) and Pinghui V. Liu. Complementation of lecithinase activities by closely related pseudomonads: its taxonomic implication. J. Bacteriol. 86:585–592. 1963.—A lecithinase activity was demonstrated by a mixture of cell-free extracts from two strains of closely related pseudomonads, neither of which was able to show this activity when grown alone. One component, from B-2265 (Pseudomonas aureofaciens var. nonliquefaciens), was heatlabile, nondialyzable, and antigenic. The other component, from 22/3 (P. fluorescens), was relatively heat-stable, nondialyzable, and nonantigenic. Antisera produced with the component of B-2265 alone neutralized the activity of the complete enzyme made up with both components, as well as that of similar enzymes of related species, such as P. aureofaciens, P. chlororaphis, and P. fluorescens. The taxonomic implication of these findings is discussed. The suggestion is made that determination of the serological specificity of an enzyme or its antigenic subunits is a more reliable criterion for establishing relationships of bacterial strains than methods depending on the overall similarity of biochemical activities.

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Selected References

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

  1. COSTLOW R. D. Lecithinase from Bacillus anthracis. J Bacteriol. 1958 Sep;76(3):317–325. doi: 10.1128/jb.76.3.317-325.1958. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Crawford I. P., Yanofsky C. ON THE SEPARATION OF THE TRYPTOPHAN SYNTHETASE OF ESCHERICHIA COLI INTO TWO PROTEIN COMPONENTS. Proc Natl Acad Sci U S A. 1958 Dec 15;44(12):1161–1170. doi: 10.1073/pnas.44.12.1161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. ESSELMANN M. T., LIU P. V. Lecithinase production by gramnegative bacteria. J Bacteriol. 1961 Jun;81:939–945. doi: 10.1128/jb.81.6.939-945.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. FINCHAM J. R., PATEMAN J. A. Formation of an enzyme through complementary action of mutant alleles in separate nuclei in a heterocaryon. Nature. 1957 Apr 6;179(4562):741–742. doi: 10.1038/179741a0. [DOI] [PubMed] [Google Scholar]
  5. GILLESPIE W. A., ALDER V. G. Production of opacity in egg-yolk media by coagulase-positive staphylococci. J Pathol Bacteriol. 1952 Jan;64(1):187–200. doi: 10.1002/path.1700640119. [DOI] [PubMed] [Google Scholar]
  6. HUENNEKENS F. M., HANAHAN D. J., UZIEL M. Paper chromatography of lecithins. J Biol Chem. 1954 Jan;206(1):443–447. [PubMed] [Google Scholar]
  7. LEVINE C., CHARGAFF E. Procedures for the microestimation of nitrogenous phosphatide constituents. J Biol Chem. 1951 Oct;192(2):465–479. [PubMed] [Google Scholar]
  8. LIU P. V., ABE Y., BATES J. L. The roles of various fractions of Pseudomonas aeruginosa in its pathogenesis. J Infect Dis. 1961 Mar-Apr;108:218–228. doi: 10.1093/infdis/108.2.218. [DOI] [PubMed] [Google Scholar]
  9. LIU P. V. Identification of pathogenic pseudomonads by extracellular antigens. J Bacteriol. 1961 Jan;81:28–35. doi: 10.1128/jb.81.1.28-35.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LIU P. V. Survey of hemolysin production among species of pseudomonads. J Bacteriol. 1957 Dec;74(6):718–727. doi: 10.1128/jb.74.6.718-727.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. MONSOUR V., COLMER A. R. The action of some members of the genus serratia on egg yolk complex. J Bacteriol. 1952 May;63(5):597–603. doi: 10.1128/jb.63.5.597-603.1952. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. McClung L. S., Toabe R. The Egg Yolk Plate Reaction for the Presumptive Diagnosis of Clostridium sporogenes and Certain Species of the Gangrene and Botulinum Groups. J Bacteriol. 1947 Feb;53(2):139–147. doi: 10.1128/jb.53.2.139-147.1947. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. SNEATH P. H. The application of computers to taxonomy. J Gen Microbiol. 1957 Aug;17(1):201–226. doi: 10.1099/00221287-17-1-201. [DOI] [PubMed] [Google Scholar]
  14. Suskind S. R., Yanofsky C., Bonner D. M. ALLELIC STRAINS OF Neurospora LACKING TRYPTOPHAN SYNTHETASE: A PRELIMINARY IMMUNOCHEMICAL CHARACTERIZATION. Proc Natl Acad Sci U S A. 1955 Aug 15;41(8):577–582. doi: 10.1073/pnas.41.8.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. WILLIS A. T., GOWLAND G. Some observations on the mechanism of the Nagler reaction. J Pathol Bacteriol. 1962 Jan;83:219–226. [PubMed] [Google Scholar]
  16. YANOFSKY C. The tryptophan synthetase system. Bacteriol Rev. 1960 Jun;24(2):221–245. doi: 10.1128/br.24.2.221-245.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]

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