Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1964 Sep;88(3):559–565. doi: 10.1128/jb.88.3.559-565.1964

PARTIAL PURIFICATION OF THE EXTRACELLULAR HEMOLYSIN OF PSEUDOMONAS AERUGINOSA

Richard S Berk 1
PMCID: PMC277347  PMID: 14208488

Abstract

Berk, Richard S. (Wayne State University, College of Medicine, Detroit, Mich.). Partial purification of the extracellular hemolysin of Pseudomonas aeruginosa. J. Bacteriol. 88:559–565. 1964.—Through a series of chemical fractionation steps, the extracellular hemolysin of Pseudomonas aeruginosa was purified 126-fold with a recovery of 49%. Hemolytic activity of crude preparations was irreversibly lost upon contact with anionic exchange materials such as diethylaminoethyl Sephadex or ECTEOLA-Cellulose, but traveled with the solvent front during passage through Sephadex G-200 and carboxymethyl Sephadex. The hemolysin was soluble in water and ethanol, and was partially extractable with ether, but not with trichlorotrifluoroethane (Freon). Although normal serum and serum albumin blocked hemolytic activity, it was unaffected by trypsin, deoxyribonuclease, or ribonuclease. Partially purified hemolysin was studied in vivo, but did not exert dermonecrotic activity in mice or rabbits in the concentrations tested. Although preparations were toxic to mice, lethality appeared to be more a reflection of the nonhemolytic protein content of the preparations rather than of hemolytic activity.

Full text

PDF
564

Selected References

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

  1. BERGAMINI L. Attività mucolitica di alcuni microrganismi. Boll Ist Sieroter Milan. 1952 Sep-Oct;31(9-10):448–452. [PubMed] [Google Scholar]
  2. BERK R. S. INTRACELLULAR HEMOLYSIN OF PSEUDOMONAS AERUGINOSA. J Bacteriol. 1963 Mar;85:522–526. doi: 10.1128/jb.85.3.522-526.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. BERK R. S., NELSON E. L. Studies on mechanisms of cellular immunity. III. Effect of Pseudomonas aeruginosa on hydrolase activity of mouse monocytes. J Infect Dis. 1962 Jan-Feb;110:1–7. doi: 10.1093/infdis/110.1.1. [DOI] [PubMed] [Google Scholar]
  4. BERK R. S. Production and characterization of Pseudomon as aeruginosa hemolysin. J Bacteriol. 1962 Nov;84:1041–1048. doi: 10.1128/jb.84.5.1041-1048.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Berk R. S., Nelson E. L. EFFECT OF MICROBIAL FRACTIONS ON THE METABOLISM OF LIVER AND MONOCYTES FROM MICE. J Bacteriol. 1961 Mar;81(3):459–463. doi: 10.1128/jb.81.3.459-463.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. KOURILSKY R., RICHOU R. Recherches sur les diastases microbiennes: sur la vitesse d'élaboration des diastases gélatinolytiques et fibrinolytiques par certains germes protéolytiques. C R Hebd Seances Acad Sci. 1954 Dec 8;239(23):1712–1714. [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. 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]
  10. MANDL I., KELLER S., COHEN B. Microbial elastases. A comparative study. Proc Soc Exp Biol Med. 1962 Apr;109:923–925. doi: 10.3181/00379727-109-27379. [DOI] [PubMed] [Google Scholar]
  11. MUFTIC M. K. New medium for the detection of esterase activity of microorganisms. Enzymologia. 1954 Nov 15;17(3):123–126. [PubMed] [Google Scholar]
  12. MULL J. D., CALLAHAN W. S. ESTIMATION OF ELASTOLYTIC ACTIVITY OF STRAINS OF PSEUDOMONAS AERUGINOSA. J Bacteriol. 1963 May;85:1178–1179. doi: 10.1128/jb.85.5.1178-1179.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. ROBINSON J., THATCHER F. S., GAGNON J. Studies with staphylococcal toxins. IV. The purification and metallic requirements of specific hemolysins. Can J Microbiol. 1958 Aug;4(4):345–361. doi: 10.1139/m58-037. [DOI] [PubMed] [Google Scholar]
  14. SCHWAB J. H. An intracellular hemolysin of group A Streptococci. II. Comparative properties of intracellular hemolysin, streptolysin S, and streptolysin O. J Bacteriol. 1956 Jan;71(1):100–107. doi: 10.1128/jb.71.1.100-107.1956. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. STREITFELD M. M., HOFFMANN E. M., JANKLOW H. M. Evaluation of extracellular deoxyribonuclease activity in Pseudomonas. J Bacteriol. 1962 Jul;84:77–80. doi: 10.1128/jb.84.1.77-80.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. ZAK B., COHEN J. Automatic analysis of tissue culture proteins with stable Folin reagents. Clin Chim Acta. 1961 Sep;6:665–670. doi: 10.1016/0009-8981(61)90112-7. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES