An extraction resistant tensile protein in the protoplasmic matrix of Physarum

A thorough extraction of plasmodia of Physarum polycephalum by sequential treatment with 1% Triton x-100, 0.6 M KI, 4% SDS plus 7 M urea leaves behind an elastic cell ghost, which represents a cytoplasmic matrix protein arranged as a continuous network in all cell regions. The protein is present in the ectoplasm as well as in the endoplasm. The extraction-resistant ghosts reveal filaments 2-3 nm in diameter, perform a conspicuous volume condensation upon the addition of mM-concentrations of di- and trivalent cations and can be partially solubilized in 4.5 M guanidinium chloride plus 25% 2-mercaptoethanol at 70 degrees C. SDS-gel electrophoresis shows a distinct band at 43,000 daltons and a faint high molecular weight component suggesting a similarity to muscle connection.