Similarities in the heavy and light chains of tetanus toxin suggested by their amino acid compositions
- 1 March 1983
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 209 (3) , 897-899
- https://doi.org/10.1042/bj2090897
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.This publication has 11 references indexed in Scilit:
- [9] Relating proteins by amino acid compositionPublished by Elsevier ,1983
- Solid‐Phase Sequence Analysis of Polypeptides Eluted from Polyacrylamide GelsEuropean Journal of Biochemistry, 1982
- Purification of tetanus toxin and its peptide components by preparative polyacrylamide gel electrophoresisArchives of Biochemistry and Biophysics, 1982
- Silver staining of proteins in polyacrylamide gelsAnalytical Biochemistry, 1981
- Plasmid-Associated Toxigenicity in Clostridium tetaniThe Journal of Infectious Diseases, 1980
- How reliably do amino acid composition comparisons predict sequence similarities between proteins?Journal of Theoretical Biology, 1979
- Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.Journal of Biological Chemistry, 1977
- Structure of tetanus toxin. II. Toxin binding to ganglioside.Journal of Biological Chemistry, 1977
- Binding of ganglioside by the chains of tetanus toxinFEBS Letters, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970