The primary structure of Clostridium perfringens ferredoxin.

Primary structure of alfalfa ferredoxin.

The amino acid sequences of the six peptides obtained from tryptic digests of alfalfa ferredoxin were determined by chemical and enzymic degradations. The order of tryptic peptides was established from the properties of the two segments of the succinylated protein obtained by tryptic hydrolysis at the single arginyl residue. Alfalfa ferredoxin consists of a polypeptide chain of 9’7 residues, ch...

Preparation of Standard Clostridium perfringens Antitoxin in the Sheep

Clostridium perfringens Iota-Toxin: Structure and Function

Clostridium perfringens iota-toxin is composed of the enzyme component (Ia) and the binding component (Ib). Ib binds to receptor on targeted cells and translocates Ia into the cytosol of the cells. Ia ADP-ribosylates actin, resulting in cell rounding and death. Comparisons of the deduced amino acid sequence from the gene and three-dimensional structure of Ia with those of ADP-ribosylating toxin...

Structure of the claudin-binding domain of Clostridium perfringens enterotoxin.

Clostridium perfringens enterotoxin is a common cause of food-borne and antibiotic-associated diarrhea. The toxin's receptors on intestinal epithelial cells include claudin-3 and -4, members of a large family of tight junction proteins. Toxin-induced cytolytic pore formation requires residues in the NH(2)-terminal half, whereas residues near the COOH terminus are required for binding to claudin...

Bacteriophages of Clostridium perfringens