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Literature DB >> 6870797

Similarities in the heavy and light chains of tetanus toxin suggested by their amino acid compositions.

Abstract

Quantitative comparison of the amino acid compositions of the heavy and light chains of tetanus toxin by the method of Cornish-Bowden [(1983) Methods Enzymol. 91, 60-75)] suggests strongly that there is sequence homology between the two chains and that the heavy chain has two similar halves. Examination (by electrophoresis in polyacrylamide gels in the presence of sodium dodecyl sulphate) of peptides produced from the chains by proteolytic cleavage supports this idea.

Entities: Chemical Disease

Mesh：

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Year: 1983 PMID： 6870797 PMCID： PMC1154173 DOI： 10.1042/bj2090897

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

9 in total

1. Binding of ganglioside by the chains of tetanus toxin.

Authors: S van Heyningen
Journal: FEBS Lett Date: 1976-09-15 Impact factor: 4.124

2. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

Authors: D W Cleveland; S G Fischer; M W Kirschner; U K Laemmli
Journal: J Biol Chem Date: 1977-02-10 Impact factor: 5.157

3. How reliably do amino acid composition comparisons predict sequence similarities between proteins?

Authors: A Cornish-Bowden
Journal: J Theor Biol Date: 1979-02-21 Impact factor: 2.691

4. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors: U K Laemmli
Journal: Nature Date: 1970-08-15 Impact factor: 49.962

5. Solid-phase sequence analysis of polypeptides eluted from polyacrylamide gels. An aid to interpretation of DNA sequences exemplified by the Escherichia coli unc operon and bacteriophage lambda.

Authors: J E Walker; A D Auffret; A Carne; A Gurnett; P Hanisch; D Hill; M Saraste
Journal: Eur J Biochem Date: 1982-04-01

6 in total

Review 1. Properties and use of botulinum toxin and other microbial neurotoxins in medicine.

Authors: E J Schantz; E A Johnson
Journal: Microbiol Rev Date: 1992-03

2. Failure of analysis of amino acid composition as a probe for sequence similarity in tetanus toxin.

Authors: S van Heyningen; A F Coulson
Journal: Biochem J Date: 1987-06-15 Impact factor: 3.857

3. Enzymatic hydrolysis of tetanus toxin by intrinsic and extrinsic proteases. Characterization of the fragments by monoclonal antibodies.

Authors: K Goretzki; E Habermann
Journal: Med Microbiol Immunol Date: 1985 Impact factor: 3.402

Similarities in the heavy and light chains of tetanus toxin suggested by their amino acid compositions.

1. Binding of ganglioside by the chains of tetanus toxin.

2. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

3. How reliably do amino acid composition comparisons predict sequence similarities between proteins?

4. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

5. Solid-phase sequence analysis of polypeptides eluted from polyacrylamide gels. An aid to interpretation of DNA sequences exemplified by the Escherichia coli unc operon and bacteriophage lambda.

6. Structure of tetanus toxin. II. Toxin binding to ganglioside.

7. Relating proteins by amino acid composition.

8. Purification of tetanus toxin and its peptide components by preparative polyacrylamide gel electrophoresis.

9. Plasmid-associated toxigenicity in Clostridium tetani.

Review 1. Properties and use of botulinum toxin and other microbial neurotoxins in medicine.

2. Failure of analysis of amino acid composition as a probe for sequence similarity in tetanus toxin.

3. Enzymatic hydrolysis of tetanus toxin by intrinsic and extrinsic proteases. Characterization of the fragments by monoclonal antibodies.

4. Antibodies against the light chain of tetanus toxin in human sera.

5. The amino acid compositions of proteins are correlated with their molecular sizes.

6. Tetanus toxin: primary structure, expression in E. coli, and homology with botulinum toxins.