Abstract
This chapter describes the production and purification of cholera toxin. Cholera toxin (choleragen, permeability factor, cholera enterotoxin) is an extracellularly secreted protein produced by toxinogenic strains of Vibrio cholerae . Cholera toxin (CT) is highly related to the heat-labile enterotoxin (LT) of Escherichia coli in structure and activity. This family of enterotoxins causes diarrhea through the activation of adenylate cyclase and the alteration of ion transport in intestinal epithelial cells. CT is composed of two types of subunits, A (MW 27,215) and B (MW 11,677), which are present in the native molecule in a ratio of 1: 5, respectively. The A subunit is composed of two disulfide-linked peptides A1 (MW 21,817) and A2 (MW 5398). These two peptides are derived from a common precursor by an internal proteolytic cleavage or nick that occurs after extracellular secretion of the holotoxin. CT purified by the method described in the chapter is available from several commercial sources. These commercial preparations as well as freshly prepared CT retain high biological activity.
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