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Electrophoretic analysis of actin, obtained within 1.2 and 5 days after death, did not exhibit any destructions of the protein. At the same time, an ability of actin to develop the actomyosin complex was decreased during autolysis as shown by affinity chromatography of actin on CNBr-Sepharose containing immobilized myosin. Alterations in fluorescence spectra of the actin preparations enabled to suggest that an increase of inactive, unable to polymerization form of the protein during autolysis was responsible for reduction of its property to associate with myosin.
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