Separation of toxic activity and ADP-ribosylation activity of botulinum neurotoxin D.
Neurotoxin from Clostridium botulinum type D strain South African (neurotoxin D) has shown ADP-ribosylation activity as well as toxic activity (Matsuoka, I., Sakuma, H., Syuto, B., Moriishi, K., Kubo, S., and Kurihara, K. (1989) J. Biol. Chem. 264, 706-712). Separation of these activities from each other was attempted by means of gel filtration, hydroxylapatite column chromatography, or immunoaffinity chromatography. Approximately 90% of toxic activity was recovered in each chromatography. Although ADP-ribosylation activity was incompletely separated from neurotoxin D by gel filtration, it was separated by hydroxylapatite column chromatography. In immunoaffinity chromatography with a column of Sepharose 4B coupling antibodies against botulinum ADP-ribosyltransferase, no ADP-ribosylation activity was detected by autoradiography in the unabsorbed toxic fraction. These results indicate that neurotoxin D does not have ADP-ribosylation activity.
Moriishi
K
K
Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Syuto
B
B
Oguma
K
K
Saito
M
M
D001905:Botulinum Toxins / Q000302:isolation & purification* / Q000378:metabolism / Q000633:toxicity; D002845:Chromatography; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D017886:Durapatite; D006882:Hydroxyapatites; D008970:Molecular Weight; D011065:Poly(ADP-ribose) Polymerases / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity
D006882:Hydroxyapatites; D017886:Durapatite; D011065:Poly(ADP-ribose) Polymerases; D001905:Botulinum Toxins