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Literature DB >> 200566

Physical changes in the epsilon prototoxin molecule of Clostridium perfringens during enzymatic activation.

Abstract

Enzymatic activation of Clostridium perfringens epsilon prototoxin removed a small basic part of the molecule, causing a slight change in molecular weight (32,700 to 31,200) and a large change in isoelectric point (from pH 8.02 into fractions of 5.36 and 5.74).

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Year: 1977 PMID： 200566 PMCID： PMC421267 DOI： 10.1128/iai.18.2.549-551.1977

Source DB: PubMed Journal: Infect Immun ISSN： 0019-9567 Impact factor: 3.441

1 in total

1. Studies on epsilon-prototoxin of Clostridium perfringens type D. I. Purification methods: evidence for multiple forms of epsilon-prototoxin.

Authors: A F Habeeb
Journal: Arch Biochem Biophys Date: 1969-03 Impact factor: 4.013

1 in total

13 in total

1. Cloning and nucleotide sequencing of the Clostridium perfringens epsilon-toxin gene and its expression in Escherichia coli.

Authors: S E Hunter; I N Clarke; D C Kelly; R W Titball
Journal: Infect Immun Date: 1992-01 Impact factor: 3.441

2. Identification of tyrosine 71 as a critical residue for the cytotoxic activity of Clostridium perfringens epsilon toxin towards MDCK cells.

Authors: Zhigang Jiang; Jitao Chang; Fang Wang; Li Yu
Journal: J Microbiol Date: 2015-01-28 Impact factor: 3.422

3. F199E substitution reduced toxicity of Clostridium perfringens epsilon toxin by depriving the receptor binding capability.

Authors: Jingjing Kang; Jie Gao; Wenwu Yao; Lin Kang; Shan Gao; Hao Yang; Bin Ji; Ping Li; Jing Liu; Jiahao Yao; Wenwen Xin; Baohua Zhao; Jinglin Wang
Journal: Hum Vaccin Immunother Date: 2017-03-17 Impact factor: 3.452

4. A low-toxic site-directed mutant of Clostridium perfringens ε-toxin as a potential candidate vaccine against enterotoxemia.

Authors: Qing Li; Wenwen Xin; Shan Gao; Lin Kang; Jinglin Wang
Journal: Hum Vaccin Immunother Date: 2013-07-08 Impact factor: 3.452

5. Identification of amino acids important for binding of Clostridium perfringens epsilon toxin to host cells and to HAVCR1.

Authors: Susan E Ivie; Mark S McClain
Journal: Biochemistry Date: 2012-09-12 Impact factor: 3.162

Physical changes in the epsilon prototoxin molecule of Clostridium perfringens during enzymatic activation.

1. Studies on epsilon-prototoxin of Clostridium perfringens type D. I. Purification methods: evidence for multiple forms of epsilon-prototoxin.

1. Cloning and nucleotide sequencing of the Clostridium perfringens epsilon-toxin gene and its expression in Escherichia coli.

2. Identification of tyrosine 71 as a critical residue for the cytotoxic activity of Clostridium perfringens epsilon toxin towards MDCK cells.

3. F199E substitution reduced toxicity of Clostridium perfringens epsilon toxin by depriving the receptor binding capability.

4. A low-toxic site-directed mutant of Clostridium perfringens ε-toxin as a potential candidate vaccine against enterotoxemia.

5. Identification of amino acids important for binding of Clostridium perfringens epsilon toxin to host cells and to HAVCR1.

6. Functional analysis of neutralizing antibodies against Clostridium perfringens epsilon-toxin.

Review 7. Clostridium perfringens type A-E toxin plasmids.

8. Effect of Clostridium perfringens epsilon toxin on the cardiovascular system of rats.

9. The Myelin and Lymphocyte Protein MAL Is Required for Binding and Activity of Clostridium perfringens ε-Toxin.

10. Clostridium Perfringens Toxins Involved in Mammalian Veterinary Diseases.