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[The C-terminal fragment of thymopoietin forms F-actin bundles: electron microscopic data].

It was shown by electron microscopy that PEP33 a synthetic C-terminal peptide of the thymus hormone thymopoietin, formed bundles of actin 'filaments in the presence of 0.1 M KCl. The structure of PEP33 aggregates localizated in the bundles between actin filaments is very similar to that of aggregates observed in samples of pure PEP33. No changes were revealed in the structure of G-actin in the presence of PEP33. A similar, but a weaker bundling effect of thymopentin (PEP5) was also found. It forms bundles of actin filaments of small size. Further studies can shed light on the physiological importance of actin filament aggregation with the peptides of thymopoietin, the systematic release of which from the thymus produces the phenomena characteristic for the serious neuromuscular disease myasthenia gravis.