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| CAS No.: | 9012-63-9 |
|---|---|
| Name: | CHOLERA TOXIN |
| Molecular Structure: | |
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| Formula: | NULL |
| Molecular Weight: | 0 |
| Synonyms: | Choleratoxin; Cholera toxins; Choleragen; Choleragenoid; Toxins, exo-, cholera |
| Safety: | A poison by intravenous route. Experimental reproductive effects. Mutation data reported. When heated to decomposition it emits acrid smoke and irritating vapors. |
| PSA: | 0.00000 |
| LogP: | 0.00000 |
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Chemistry
Chemistry informtion about Cholera Toxin (9012-63-9) is:
Synonyms: Cholera Toxin ; Cholera Enterotoxin ; Cholera Toxin, Vibrio Cholerae, Type Inaba 569b ; Vibrio Cholerae Toxin ; Choleraentero-Exotoxin ; Choleraexotoxin ; Choleragen ; Exo-Enterotoxin
Storage temp.: 0-6°C
History
The gene encoding the cholera toxin is introduced into V. cholerae by horizontal gene transfer. Virulent strains of V. cholerae carry a variant of lysogenic bacteriophage called CTXf or CTXφ.
Uses
Cholera Toxin (9012-63-9) has been used as a neuronal tracer.Also,it can be used to identify rafts.
Toxicity Data With Reference
| 1. | dns-mus-oth 10 µg/L | CRNGDP Carcinogenesis. 8 (1987),377. | ||
| 2. | ivn-mus LD50:260 µg/kg | IMLCAV Immunological Communications. 1 (1972),223. | ||
| 3. | ivn-mky LDLo:10 µg/kg | TOXIA6 Toxicon. 18 (1980),309. | ||
| 4. | ivn-rbt LDLo:100 µg/kg | TOXIA6 Toxicon. 19 (1981),701. |
Safety Profile
A poison by intravenous route. Experimental reproductive effects. Mutation data reported. When heated to decomposition it emits acrid smoke and irritating vapors.
RIDADR: 3172
HazardClass: 6.1
PackingGroup: I
Specification
Cholera Toxin (9012-63-9) is an oligomeric complex made up of six protein subunits: a single copy of the A subunit (part A), and five copies of the B subunit (part B). The two parts are connected by a disulfide bond. The three-dimensional structure of the toxin was determined using X-ray crystallography by Zhang et al. in 1995. The five B subunits—each weighing 12 kDa, and all coloured blue in the accompanying figure—form a five-membered ring. The A subunit has two important segments. The A1 portion of the chain (CTA1, red) is a globular enzyme payload that ADP-ribosylates G proteins, while the A2 chain (CTA2, orange) forms an extended alpha helix which seats snugly in the central pore of the B subunit ring.This structure is similar in shape, mechanism, and sequence to the heat-labile enterotoxin secreted by some strains of the Escherichia coli bacterium.