Infect Immun. 1986 August; 53(2): 435-437
Composition of affinity-purified alpha-hemolysin of Escherichia coli.
G A Bohach and
I S Snyder
ABSTRACT
Escherichia coli alpha-hemolysin was purified from culture supernatants by affinity chromatography, using a hemolysis-neutralizing monoclonal antibody ligand. Purified hemolysin contains several proteins and lipopolysaccharides. Thus, alpha-hemolysin exists as a macromolecular complex and may be exported from E. coli cells by outer membrane fragmentation.
Infect Immun. 1986 August; 53(2): 435-437
This article has been cited by other articles:
-
Billson, F. M., Harbour, C., Michalski, W. P., Tennent, J. M., Egerton, J. R., Hodgson, J. L.
(2000). Characterization of Hemolysin of Moraxella bovis Using a Hemolysis-Neutralizing Monoclonal Antibody. Infect. Immun.
68: 3469-3474
[Abstract]
[Full Text]
-
Curtis, M. A., Thickett, A., Slaney, J. M., Rangarajan, M., Aduse-Opoku, J., Shepherd, P., Paramonov, N., Hounsell, E. F.
(1999). Variable Carbohydrate Modifications to the Catalytic Chains of the RgpA and RgpB Proteases of Porphyromonas gingivalis W50. Infect. Immun.
67: 3816-3823
[Abstract]
[Full Text]
-
Gleason, T. G., Houlgrave, C. W., May, A. K., Crabtree, T. D., Sawyer, R. G., Denham, W., Norman, J. G., Pruett, T. L.
(1998). Hemolytically Active (Acylated) Alpha-Hemolysin Elicits Interleukin-1beta (IL-1beta ) but Augments the Lethality of Escherichia coli by an IL-1- and Tumor Necrosis Factor-Independent Mechanism. Infect. Immun.
66: 4215-4221
[Abstract]
[Full Text]
Copyright © 1986 by the American Society for Microbiology. All rights reserved.