Abstract
Lethal toxin was purified extensively from the culture filtrate of a Kanagawa phenomenon-positive strain of Vibrio parahaemolyticus. The purified toxin was a protein, and its homogeneity was demonstrated by sodium dodecyl sulfate-polyacrylamide gel disc electrophoresis and analytical ultracentrifugation. It was demonstrated that the thermostable direct hemolysin was identical to the lethal toxin and that it was the main, if not only, lethal toxin in the culture filtrate. The purified toxin had a lethal effect when injected into mice either intravenously or intraperitoneally. Its lethal effect was very rapid, a dose of 5 mug of toxin per mouse killing the animals within 1 min. The lethal activity was inhibited by a ganglioside mixture. Some physicochemical properties of the purified toxin are reported.
Full text
PDF






Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Baginski E. S., Foà P. P., Zak B. Microdetermination of inorganic phosphate, phospholipids, and total phosphate in biologic materials. Clin Chem. 1967 Apr;13(4):326–332. [PubMed] [Google Scholar]
- Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
- Honda T., Goshima K., Takeda Y., Sugino Y., Miwatani T. Demonstration of the cardiotoxicity of the thermostable direct hemolysin (lethal toxin) produced by Vibrio parahaemolyticus. Infect Immun. 1976 Jan;13(1):163–171. doi: 10.1128/iai.13.1.163-171.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Miyamoto Y., Kato T., Obara Y., Akiyama S., Takizawa K., Yamai S. In vitro hemolytic characteristic of Vibrio parahaemolyticus: its close correlation with human pathogenicity. J Bacteriol. 1969 Nov;100(2):1147–1149. doi: 10.1128/jb.100.2.1147-1149.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Morris D. L. Quantitative Determination of Carbohydrates With Dreywood's Anthrone Reagent. Science. 1948 Mar 5;107(2775):254–255. doi: 10.1126/science.107.2775.254. [DOI] [PubMed] [Google Scholar]
- Niikawa T., Obara Y., Yamai S., Miyamoto Y. Purification of a hemolysin from Vibrio parahaemolyticus. Jpn J Med Sci Biol. 1972 Jun;25(3):197–200. [PubMed] [Google Scholar]
- Sakurai J., Matsuzaki A., Miwatani T. Purification and characterization of thermostable direct hemolysin of Vibrio parahaemolyticus. Infect Immun. 1973 Nov;8(5):775–780. doi: 10.1128/iai.8.5.775-780.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sakurai J., Matsuzaki A., Takeda Y., Miwatani T. Existence of two distinct hemolysins in Vibrio parahaemolyticus. Infect Immun. 1974 May;9(5):777–780. doi: 10.1128/iai.9.5.777-780.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Takeda R., Honda T., Sakural J., Otomo N. Inhibition of hemolytic activity of the thermostable direct hemolysin of Vibrio parahaemolyticus by ganglioside. Infect Immun. 1975 Oct;12(4):931–933. doi: 10.1128/iai.12.4.931-933.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Takeda Y., Hori Y., Miwatani T. Demonstration of a temperature-dependent inactivating factor of the thermostable direct hemolysin in Vibrio parahaemolyticus. Infect Immun. 1974 Jul;10(1):6–10. doi: 10.1128/iai.10.1.6-10.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zen-Yoji H., Hitokoto H., Morozumi S., Le Clair R. A. Purification and characterization o;f a hemolysin produced by Vibrio parahaemolyticus. J Infect Dis. 1971 Jun;123(6):665–667. doi: 10.1093/infdis/123.6.665. [DOI] [PubMed] [Google Scholar]

