title: Tryptophan content of Clostridium perfringens epsilon toxin.
abstract: The tryptophan content of Clostridium perfringens epsilon toxin was investigated. When the tryptophan content was determined by amino acid analysis after the hydrolysis of epsilon prototoxin with methanesulfonic acid containing 3-(2-aminoethyl)indole and by the spectrophotometric method with N-bromosuccinimide, the number of tryptophan residues was calculated at 1/mol of the protein. Cleavage of the prototoxin or the toxin with N-bromosuccinimide in the presence of urea gave two new fragments on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. There was only a tyrosine residue as the new N-terminal amino acid after the cleavage of the prototoxin or the toxin with N-bromosuccinimide. The data showed that epsilon prototoxin or epsilon toxin contained only one tryptophan residue.
authors.forename: J
authors.initials: J
authors.lastname: Sakurai
authors.forename: M
authors.initials: M
authors.lastname: Nagahama
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001427:Bacterial Toxins / Q000302:isolation & purification*; D003016:Clostridium perfringens / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D014364:Tryptophan / Q000032:analysis*
chemical_list: D000596:Amino Acids; D001427:Bacterial Toxins; C039811:Clostridium perfringens epsilon-toxin; D010446:Peptide Fragments; D014364:Tryptophan