Abstract
A thermostable direct hemolysin was purified from culture filtrates of Vibrio parahaemolyticus. The purified hemolysin gave one precipitation line with the antihemolysin antiserum on agar-gel diffusion test and a single band on polyacrylamide gel electrophoresis. The hemolysin was not inactivated by heating at 70 to 100 C for 10 min. The hemolytic activity was not enhanced by the addition of lecithin. It was demonstrated that the hemolysin was a protein with a molecular weight of approximately 118,000. Amino acid analysis revealed that 43% of total amino acids were acidic amino acids, whereas 11% were basic amino acids.
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.
- ALOUF J. E., RAYNAUD M. Purification of streptolysin O. Nature. 1962 Oct 27;196:374–375. doi: 10.1038/196374a0. [DOI] [PubMed] [Google Scholar]
- 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]
- Bernheimer A. W. Physical behavior of streptolysin S. J Bacteriol. 1967 Jun;93(6):2024–2025. doi: 10.1128/jb.93.6.2024-2025.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- CHESBRO W. R., HEYDRICK F. P., MARTINEAU R., PERKINS G. N. PURIFICATION OF STAPHYLOCOCCAL BETA-HEMOLYSIN AND ITS ACTION ON STAPHYLOCOCCAL AND STREPTOCOCCAL CELL WALLS. J Bacteriol. 1965 Feb;89:378–389. doi: 10.1128/jb.89.2.378-389.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
- Fujino T., Miwatani T., Takeda Y., Tomaru A. A thermolabile direct hemolysin of Vibrio parahaemolyticus. Biken J. 1969 Jun;12(2):145–148. [PubMed] [Google Scholar]
- Kantor H. S., Temples B., Shaw W. V. Staphylococcal delta hemolysin: purification and characterization. Arch Biochem Biophys. 1972 Jul;151(1):142–156. doi: 10.1016/0003-9861(72)90483-3. [DOI] [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]
- Miwatani T., Sakurai J., Yoshihara A., Takeda Y. Isolation and partial purification of thermolabile direct hemolysin of Vibrio parahaemolyticus. Biken J. 1972 Jun;15(2):61–66. [PubMed] [Google Scholar]
- Miwatani T., Takeda Y., Sakurai J., Yoshihara A., Taga S. Effect of heat (Arrhenius effect) on crude hemolysin of Vibrio parahaemolyticus. Infect Immun. 1972 Dec;6(6):1031–1033. doi: 10.1128/iai.6.6.1031-1033.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Miwtani T., Shinoda S., Nishimune H., Okada M., Takeda Y. A common antigenic substance of Vibrio parahaemolyticus. I. Isolation and purification. Biken J. 1969 Jun;12(2):97–106. [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]
- Yanagase Y., Inoue K., Ozaki M., Ochi T., Amano T. Hemolysins and related enzymes of Vibrio parahaemolyticus. I. Identification and partial purification of enzymes. Biken J. 1970 Jun;13(2):77–92. [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]