Partial Amino Acid Sequences of Botulinum Neurotoxins Types B and E
Abstract
Clostridium botulinum type E neurotoxin, a single chain protein of Mr 147,000, was purified and subjected to amino acid sequencing. The same done for single chain botulinum type B neurotoxin (Mr 152,000), and for the heavy and light chains (Mr 104,000 and 51,000 respectively) derived from type B by limiting trypsin digestion. Twelve to 18 residues were identified and the following conclusions were drawn: (1) The light chain of the nicked (dichain) type B is derived from the N-terminal one third of the single chain (unnicked) parent neurotoxin (2) sequence homologies are present better single chain types B and E and the light chain of the nicked type A, (3) the N-terminal regions of the heavy chains of types A and B have some structural similarity: (4) activation of type B neurotoxin cannot involve removal of amino acids or peptides for the N-terminus.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1984
- Accession Number
- ADA146643
Entities
People
- Bibhuti R. Dasgupta
- James J. Schmidt
- Venugopal Sathyamoorthy
Organizations
- United States Army Medical Research Institute of Infectious Diseases