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9012-63-9

Basic Information
CAS No.: 9012-63-9
Name: Toxins, cholera
Molecular Structure:
Molecular Structure of 9012-63-9 (Toxins, cholera)
Formula: NULL
Molecular Weight: 0
Synonyms: Choleratoxin; Cholera toxins; Choleragen; Choleragenoid; Toxins, exo-, cholera
EINECS:
Density:
Melting Point:
Boiling Point:
Flash Point:
Solubility:
Appearance:
Hazard Symbols:
Risk Codes:
Safety: A poison by intravenous route. Experimental reproductive effects. Mutation data reported. When heated to decomposition it emits acrid smoke and irritating vapors.
Transport Information:
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.