[1] Through SDS-PAGE analysis, TCX (112154-17-3 ) was determined to be a complex held together by non-covalent forces of the following three polypeptides in a stoichiometry of 1:1:4 respectively:[2] The active complex was isolated by ion exchange chromatography through DE-Cellulose and two steps of Cm-Cellulose chromatography at pH = 4.7 and pH = 6.0, respectively.
The alpha-neurotoxin-like peptide can be separated from the protease inhibitor, Sephadex G-50 gel filtration chromatography can be used, in the presence of high salt (1M NaCl) and alkaline conditions (pH = 8.2).
The amino sequence of the protease inhibitor was determined by using the automatic Edman degradation method.
[5] It has a high affinity for the 125I-apamin acceptor-binding sites of the rat synaptosomal membranes (Ki = 1.45±0.22 nM) and blocks affinity-labeling of a 33-kDa 125I-apamin-binding polypeptide.
It lowers the plateau of the action potential, decreasing the duration and the concentration parameters in the heart muscle cells.