Purification and characterization of thermostable direct hemolysin of Vibrio parahaemolyticus.

Infection and immunity ·Vol. 8 ·No. 5 ·1973-11-00 ·Pages 775-80

Sakurai J, Matsuzaki A, Miwatani T

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.

MeSH Terms

Amino Acids/analysis Animals Antibodies, Anti-Idiotypic Antibodies, Bacterial/isolation & purification Autoanalysis Carbohydrates/analysis Chromatography Chromatography, DEAE-Cellulose Chromatography, Gel Dextrans Electrophoresis, Polyacrylamide Gel Erythrocytes/immunology Hemolysin Proteins/isolation & purification Hemolysis Hot Temperature Humans Immune Sera Immunodiffusion Molecular Weight Pepsin A Rabbits/immunology Trypsin Vibrio/immunology

Chemicals

Amino Acids Antibodies, Anti-Idiotypic Antibodies, Bacterial Carbohydrates Dextrans Hemolysin Proteins Immune Sera Trypsin Pepsin A

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Sakurai J

Matsuzaki A

Miwatani T

References (15)

15 references, click to expand

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Article Info

Journal

Infection and immunity

Abbr.

Infect Immun

ISSN

0019-9567

DOI

10.1128/iai.8.5.775-780.1973

Published

1973-11-00

Pages

775-80

Language

English

Region

United States

NLM ID

0246127

PMCID

PMC422926

Subset

External Links

PubMed source DOI: 10.1128/iai.8.5.775-780.1973 PMC Full Text View journal details

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Purification and characterization of thermostable direct hemolysin of Vibrio parahaemolyticus.

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