Abstract
Cholera enterotoxin, a protein secreted by the bacterium V&?o cholerae, activates adenylate cyclase in a wide variety of vertebrate cell types [l] . The toxin consists of two different types of subunit, known as the A (‘active’) and B (‘binding’) subunits, associated in non-covalent fashion [ 21. Each toxin molecule probably contains one A and five B subunits [3]. Under suitable conditions the A subunit is sufficient to activate adenylate cyclase in plasma membrane fragments [4,5]. The B subunit has a strong affinity for G,, ganglioside in plasma membranes, and this interaction seems to be necessary for the function of the toxin in intact cells [6]. Nearly all the antigenicity of the intact toxin resides in the B subunit [2]. We have determined the primary structure of the B subunit as a step toward understanding structure-function relationships in cholera enterotoxin.
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