Application
The toxin is released from B. pertussis in an inactive form. When the pertussis toxin B oligomer binds to the cell membrane, the S1 subunit of its A protomer becomes activated, perhaps through the action of glutathione and ATP. A protocol for activating pertussis toxin in vitro is given by Kaslow, et al.
Biochem/physiol Actions
Pertussis toxin catalyzes the ADP-ribosylation of the α subunits of the heterotrimeric guanine nucleotide regulatory proteins Gi, Go, and Gt. This prevents the G protein heterotrimers from interacting with receptors, thus blocking their coupling and activation. Since the Gα subunits remain in their GDP-bound, inactive state, they are unable to inactivate adenylyl cyclase or open K+ channels.
Features and Benefits
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Physical form
Aseptically filled solution in 50% glycerol, containing 50 mM TRIS, 10 mM glycine, 0.5 M NaCl, pH 7.5
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