Description
Tetanus toxin is an extremely potent neurotoxin produced by the vegetative cell of Clostridium tetani in anaerobic conditions, causing tetanus. It has no known function for clostridia in the soil environment where they are normally encountered. It is also called spasmogenic toxin, tetanospasmin or abbreviated to TeTx or TeNT. The tetanus toxin protein has a molecular weight of 150kDa. It is translated from the TetX gene as one protein which is subsequently cleaved into two parts: a 100kDa heavy or B-chain and a 50kDa light or A-chain. The chains are connected by a disulfide bond. The Bchain binds to dissialogangliosides (GD2 and GD1b) on the neuronal membrane and contains a translocation domain which aids the movement of the protein across that membrane and into the neuron. The A-chain, a zinc endopeptidase, attacks the vesicle-associated membrane protein (VAMP).
The light chain is a zinc endopeptidase, activated by enzymes in the cytosol that cleave the disulfide bond between the heavy and light chain. Once activated, the light chain cleaves synaptobrevin 2, blocking release of inhibitory transmitters GABA and glycine to motor neurons, causing the prolonged muscle transactions symptomatic of tetanus.
Purified Tetanus toxin is obtained from C. tetani (>95%) and then inactivated by formaldehyde
The product must be treated as potentially toxic and care taken in using and handling of this product. This product should only be handled by qualified lab personnel.
Loading ......
