Clostridium difficile toxin B: characterization and sequence of three peptides.
The cytotoxin, also named toxin B, was isolated from a toxigenic strain of Clostridium difficile, purified to homogeneity and partially characterized. The purification procedure included ultrafiltration followed by anion-exchange chromatography. We noticed that a non-specific nucleic material eluted with the protein during the purification. The presence of these nucleic acids appeared to be important for the toxic activity of the protein. Some characteristics of the cytotoxin were examined, especially the amino acid composition and the sequence of three tryptic fragments.
Bisseret
F
F
Institut de Bactériologie de la Faculté de Médecine, Strasbourg, France.
Keith
G
G
Rihn
B
B
Amiri
I
I
Werneburg
B
B
Girardot
R
R
Baldacini
O
O
Green
G
G
Nguyen
V K
VK
Monteil
H
H
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001345:Autoradiography; D001426:Bacterial Proteins; D001427:Bacterial Toxins / Q000032:analysis / Q000302:isolation & purification*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis*; D012836:Silver Proteins; D013194:Staining and Labeling
D000596:Amino Acids; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D010455:Peptides; D012836:Silver Proteins; C031815:toxB protein, Clostridium difficile