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[13] Purification of tetanus toxin and its major peptides

1988; Academic Press; Linguagem: Inglês

10.1016/s0076-6879(88)65016-6

1557-7988

John P. Robinson,

Biochemical and Structural Characterization

This chapter describes the purification of tetanus toxin and its major peptides. Tetanus toxin is a neurotoxic protein that contains no lipid or carbohydrate. It is produced by the anaerobic bacterium Clostridium tetani that can infect wounds under favorable conditions. The toxin acts by binding to gangliosides at the presynaptic membrane of certain synapses and blocking the release of transmitter substance. The usual assay for tetanus toxin preparations is done in mice. The growth medium for tetanus toxin contains no proteins and this simplifies the problem of separating tetanus toxin from other proteins in the culture filtrate. The uncleaved (cell extract) toxin can be prepared by hypertonic extraction from cells near the end of exponential growth phase. The protease-cleaved toxin (filtrate toxin) is prepared from older culture filtrates. This preparative electrophoresis system is not only useful for preparing the major toxin peptides; it can also be used to prepare the proteasecleaved and -uncleaved toxins in a state of high purity.