Abstract
Cytoplasmic actomyosins purified from the acellular slime mold Physarum polycephalum by application of two different procedures ( Hatano and Tazawa, 1968, Kohama and Kendrick-Jones, 1986) were compared by SDS-PAGE and contraction experiments. In contrast to the ‘Hatano actomyosin’, ‘Kohama actomyosin’ contracts in a calcium sensitive manner, i.e., contraction occurs from zero calcium up to pCa4, and is inhibited at ≥pCa 3. Distinct differences in SDS gels are discussed.
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