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. 1988 Sep;56(9):2474–2478. doi: 10.1128/iai.56.9.2474-2478.1988

Heterogeneity of hemolytic efficiency and isoelectric point of streptolysin O.

J Suzuki 1, S Kobayashi 1, K Kagaya 1, Y Fukazawa 1
PMCID: PMC259590  PMID: 3045002

Abstract

Using thin-layer agarose gel isoelectric focusing overlaid with thin-layer erythrocyte agar plates, we found that crude streptolysin O (SLO) consisted of a variety of hemolytic components with different isoelectric points (pIs) and that the distribution of pIs in crude SLO was different even in samples which were produced from a single strain of Streptococcus pyogenes under similar conditions. All of the hemolytic components in crude SLO were shown to have the properties of SLO with respect to their susceptibility to oxygen and anti-SLO serum and their molecular weight. The SLO components showed a single molecular weight of 64,000, but they exhibited various pIs ranging from pH 5.4 to 8.3, with major components showing a pI of 6 and/or 7.5. Further examination revealed the slope of the hemolytic titration curve to be dissimilar among the samples of crude SLO. Since the slope of the hemolytic titration curve of a component appears to be based on its hemolytic efficiency, the value of the slope was designated its hemolytic efficiency index. When SLO was purified by isoelectric focusing, the pI of the components was correlated with its hemolytic efficiency index; hemolytic components with lower pIs exhibited a lower hemolytic efficiency index. These results indicate that SLO consists of heterogeneous components with different pIs and suggest that the differences in hemolytic efficiency indices of SLO components are due to the different electrical charges of SLO molecules, which are related to their polymerization and affect hemolytic efficiency.

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Selected References

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

  1. Alouf J. E., Raynaud M. Purification and some properties of streptolysin O. Biochimie. 1973;55(10):1187–1193. doi: 10.1016/s0300-9084(74)80322-6. [DOI] [PubMed] [Google Scholar]
  2. Alouf J. E. Streptococcal toxins (streptolysin O, streptolysin S, erythrogenic toxin). Pharmacol Ther. 1980;11(3):661–717. doi: 10.1016/0163-7258(80)90045-5. [DOI] [PubMed] [Google Scholar]
  3. Bhakdi S., Tranum-Jensen J., Sziegoleit A. Mechanism of membrane damage by streptolysin-O. Infect Immun. 1985 Jan;47(1):52–60. doi: 10.1128/iai.47.1.52-60.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Calandra G. B., Theodore T. S. Cellular location of streptolysin O. Infect Immun. 1975 Oct;12(4):750–753. doi: 10.1128/iai.12.4.750-753.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Duncan J. L., Buckingham L. Effects of streptolysin O on transport of amino acids, nucleosides, and glucose analogs in mammalian cells. Infect Immun. 1977 Dec;18(3):688–693. doi: 10.1128/iai.18.3.688-693.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Duncan J. L. Characteristics of streptolysin O hemolysis: kinetics of hemoglobin and 86rubidium release. Infect Immun. 1974 Jun;9(6):1022–1027. doi: 10.1128/iai.9.6.1022-1027.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Duncan J. L., Mason L. Characteristics of streptolysin S hemolysis. Infect Immun. 1976 Jul;14(1):77–82. doi: 10.1128/iai.14.1.77-82.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Grushoff P. S., Shany S., Bernheimer A. W. Purification and properties of streptococcal nicotinamide adenine dinucleotide glycohydrolase. J Bacteriol. 1975 May;122(2):599–605. doi: 10.1128/jb.122.2.599-605.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Halpern B. N., Rahman S. Studies on the cardiotoxicity of streptolysin O. Br J Pharmacol Chemother. 1968 Mar;32(3):441–452. doi: 10.1111/j.1476-5381.1968.tb00445.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kehoe M., Timmis K. N. Cloning and expression in Escherichia coli of the streptolysin O determinant from Streptococcus pyogenes: characterization of the cloned streptolysin O determinant and demonstration of the absence of substantial homology with determinants of other thiol-activated toxins. Infect Immun. 1984 Mar;43(3):804–810. doi: 10.1128/iai.43.3.804-810.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Shany S., Grushoff P. S., Bernheimer A. W. Physical separation of streptococcal nicotinamide adenine dinucleotide glycohydrolase from streptolysin O. Infect Immun. 1973 May;7(5):731–734. doi: 10.1128/iai.7.5.731-734.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Smyth C. J., Fehrenbach F. J. Isoelectric analysis of haemolysins and enzymes from streptococci of groups A, C and G. Acta Pathol Microbiol Scand B Microbiol Immunol. 1974 Dec;82(6):860–870. doi: 10.1111/j.1699-0463.1974.tb02384.x. [DOI] [PubMed] [Google Scholar]
  13. Van Epps D. E., Andersen B. R. Streptolysin O: sedimentation coefficient and molecular weight determinations. J Bacteriol. 1969 Oct;100(1):526–527. doi: 10.1128/jb.100.1.526-527.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]

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