Some Effects of Pressure Treatment on Actomyosin Systems

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Abstract
Natural sheep skeletal muscle actomyosin, actin and myosin were pressurized at up to 150 MN/m2 for 1 h at 0.degree. C and examined 3-5 h later. Pressurization of myosin resulted in the formation of aggregates with a MW approximately that expected for a dimer; with F-actin depolymerization occurred. With actomyosin, a gel to sol transition was promoted. Viscosity and light-scattering measurements indicated that pressurization results in a large measure of disaggregation of actomyosin in solution. Pressurization of actomyosin resulted in a greater decrease in the Ca-sensitive, than in the Ca-independent, Mg2+ ATPase activity. The Ca2+ and K+-EDTA ATPase activities of myosin were inhibited to about the same extent.

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