Binding of 125I-Alpha Toxin of Staphylococcus Aureus to Erythrocytes

References

1. Arbuthnott J. P., Freer J. H., Billcliffe B. 1973; Lipid-induced polymerization of staphyloccal α-toxin. Journal of General Microbiology 75:309–319
   [Google Scholar]
2. Barei G. M., Fackrell H. B. 1979; The binding of fluorescein-labelled staphylococcal alpha toxoid to erythrocytes. Canadian Journal of Microbiology 25:1219–1226
   [Google Scholar]
3. Benheimer A. W. 1974; Interactions between membranes and cytolytic bacterial toxins. Biochimica et Biophysica Acta 344:27–50
   [Google Scholar]
4. Bernheimer A. W., Avigad L. S. 1980; Inhibition of bacterial and other cytolysins by glycophorin. FEMS Microbiology Letters 9:15–17
   [Google Scholar]
5. Bernheimer A. W., Schwartz L. L. 1963; Isolation and composition of staphylococcal alpha toxin. Journal of General Microbiology 30:455–468
   [Google Scholar]
6. Bhakdi S., Fussle R., Tranum-Jensen J. 1981; Staphyloccal α-toxin: oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles. Proceedings of the National Academy of Science (USA) 78:5475–5479
   [Google Scholar]
7. Birkbeck T. H., Chao L.-P., Arbuthnott J. P. 1974; Sensitivity of erythrocytes of marine fish to staphylococcal delta haemolysin. Proceedings of the Society for General Microbiology 1:55
   [Google Scholar]
8. Bretscher M. S. 1973; Membrane structure: some general principles. Science 181:622–629
   [Google Scholar]
9. Cassidy P. S., Harshman S. 1973; The binding of staphylococcal ¹²⁵I-α-toxin (B) to erythrocytes. Journal of Biological Chemistry 248:5545–5546
   [Google Scholar]
10. Cassidy P., Harshman S. 1976a; Studies on the binding of staphylococcal ¹²⁵I labeled α-toxin to rabbit erythrocytes. Biochemistry 15:2348–2355
    [Google Scholar]
11. Cassidy P., Harshman S. 1976b; Purification of staphylococcal alpha-toxin by adsorption chromatography on glass. Infection and Immunity 13:982–986
    [Google Scholar]
12. Cassidy P., Harshman S. 1979; Characterization of detergent-solubilized iodine-125-labeled α-toxin bound to rabbit erythrocytes and mouse diaphragm muscle. Biochemistry 18:232–236
    [Google Scholar]
13. Chao L.-P., Birkbeck T. H. 1978; Assay of staphylococcal δ-haemolysin with fish erythrocytes. Journal of Medical Microbiology 11:303–313
    [Google Scholar]
14. Cooper L. Z., Madoff M. A., Weinstein L. 1966; Heat stability and species range of purified staphylococcal α-toxin. Journal of Bacteriology 91:1686–1692
    [Google Scholar]
15. Dalen A. B. 1976; Proteolytic degradation of staphylococcal α-toxin. Acta Pathologica et Microbiologica Scandinavica B84:309–314
    [Google Scholar]
16. England B. J., Gunn R. B., Steck T. L. 1980; An immunological study of band 3, the anion transport protein of the human red blood cell membrane. Biochimica et Biophysica Acta 623:171–182
    [Google Scholar]
17. Freer J. H. 1982; Cytolytic toxins and surface activity. Toxicon 20:217–221
    [Google Scholar]
18. Freer J. H., Arbuthnott J. P., Bernheimer A. W. 1968; Interaction of staphylococcal α-toxin with artificial and natural membranes. Journal of Bacteriology 95:1153–1168
    [Google Scholar]
19. Freer J. H., Arbuthnott J. P., Billcliffe B. 1973; Effects of staphyloccal α-toxin on the structure of erythrocyte membranes: a biochemical and freeze-etching study. Journal of General Microbiology 75:321–332
    [Google Scholar]
20. Füssle R., Bhakdi S., Sziegoleit A., Tranum-Jensen J., Kranz T., Wellensiek H.-J. 1981; On the mechanism of membrane damage by Staphylococcus aureus α-toxin. Journal of Cell Biology 91:83–94
    [Google Scholar]
21. Hubbard A. L., Cohn Z. A. 1972; The enzymatic iodination of the red cell membrane. Journal of Cell Biology 55:390–405
    [Google Scholar]
22. Inoue M., Mori M., Seno S., Utsumi K., Yasuda T. 1974; Structural difference in sites on surface membrane of mature and immature erythrocytes. Nature 250:247–248
    [Google Scholar]
23. Inoue M., Okajima K., Ito K., Utsumi K., Seno S. 1977; Changes in structural organization of surface membrane during erythrocyte maturation. Biochimica et Biophysica Acta 467:130–136
    [Google Scholar]
24. Kato I., Sakoda K., Saito M., Suzuki Y., Watanabe M. 1975a; Studies on the haemolytic action of staphylococcal alpha toxin. Japanese Journal of Medical Science and Biology 28:332–334
    [Google Scholar]
25. Kato I., Sakoda K., Saito M., Suzuki Y., Watanabe M. 1975b; Inhibitory effect of flavin mononucleotide on the hemolysis of rabbit erythrocytes by staphylococcal alpha-toxin. Infection and Immunity 12:696–697
    [Google Scholar]
26. Kato I., Sakoda K., Saito M., Suzuki Y. 1977; Effects of lectins on the haemolysis of rabbit erythrocytes by staphylococcal alpha toxin. Microbiology and Immunology 21:517–524
    [Google Scholar]
27. Kimelberg H. K., Papahadjopoulos D. 1971; Phospholipid-protein interactions: membrane permeability correlated with monolayer “penetration”. Biochimica et Biophysica Acta 233:805–809
    [Google Scholar]
28. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
    [Google Scholar]
29. Lo C. Y., Fackrell H. B. 1979; Immunologic evidence that staphylococcal alpha toxin is oriented on membranes. Canadian Journal of Microbiology 25:686–692
    [Google Scholar]
30. Lominski I., Arbuthnott J. P. 1962; Some characteristics of staphylococcus α-haemolysin. Journal of Pathology 83:515–520
    [Google Scholar]
31. Low D. K. R., Freer J. H., Arbuthnott J. P., Möllby R., Wadstrom T. 1974; Consequences of sphingomyelin degradation in erythrocyte ghost membrane by staphylococcal β-toxin (sphingomyelinase C). Toxicon 12:279–285
    [Google Scholar]
32. Maharaj I., Fackrell H. B. 1980; Rabbit erythrocyte band 3,a receptor for staphylococcal alpha toxin. Canadian Journal of Microbiology 26:524–531
    [Google Scholar]
33. Reisfeld R. A., Lewis U. J., Williams D. E. 1962; Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature 195:281–283
    [Google Scholar]
34. Skutelsky E., Lotan R., Sharon N., Danon D. 1977; Distribution of the T-antigen on erythroid cell surfaces. Studies with peanut agglutinin, an anti-T specific lectin. Biochimica et Biophysica Acta 467:165–174
    [Google Scholar]
35. Tomarelli R. M., Charney J., Harding M. L. 1949; The use of azoalbumin as a substrate in the colorimetric determination of peptic and tryptic activity. Journal of Laboratory and Clinical Medicine 34:428–433
    [Google Scholar]
36. Weber K., Osborn M. 1969; The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244:4406–4412
    [Google Scholar]