No abstract

Intact cholera toxin and its purified subunit A both activate the adenylate cyclase of pigeon erythrocyte membranes, but subunit B does not. The activation by subunit A is unaffected by treatments that inhibit whole toxin by interfering with the binding of subunit B to cell membranes.

No abstract

No abstract

Choleragenoid binds more slowly and less strongly than cholera toxin to intestinal mucosal cells, and even less strongly to free ganglioside in solution. However, binding to ganglioside is greatly enhanced when the ganglioside is in the form of an insoluble complex with cerebroside. These findings suggest that both the binding and the active components of the toxin molecule may be necessary for optimal binding of the toxin to the intact cell, and that the ganglioside in the cell receptor is in a complex form. Choleragenoid only partially blocks the action of the toxin on ruptured cells. This observation indicates that, while binding to a membrane receptor is necessary for the action of the toxin on the whole cell, it is possible to activate adenyl cyclase in a perforated cell by a process apparently independent of membrane binding; however, this activation may be possible only if the toxin preparation contains the active component dissociated from choleragenoid.