Abstract
Choleragen (cholera toxin) exerts its effects on animal cells by activating adenylate cyclase, thereby increasing intracellular cAMP content (1). The A1 protein of choleragen, released from the holotoxin by reduction of a single disulfide bond linking the A1 and A2 proteins, catalyzes the mono- ADP-ribosylation of Gsα, a regulatory component of the adenylate cyclase system that is responsible for the GTP-dependent activation of the cyclase catalytic unit. ADP-ribosylation of Gsα apparently increases its sensitivity to GTP and its dissociation from the inhibitory Gβγ complex (1).
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© 1989 Springer-Verlag New York Inc.
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Noda, M. et al. (1989). Activation of the NAD Glycohydrolase, NAD:Agmatine and NAD:Gsα ADP-Ribosyltransferase and Auto-ADP-Ribosylation Activities of Choleragen by Guanyl Nucleotide and Soluble Proteins Purified from Bovine Brain. In: Jacobson, M.K., Jacobson, E.L. (eds) ADP-Ribose Transfer Reactions. Springer, New York, NY. https://doi.org/10.1007/978-1-4615-8507-7_86
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DOI: https://doi.org/10.1007/978-1-4615-8507-7_86
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