Effects of pressure treatment on the ultrastructure of striated muscle

Pre- and post-rigor sheep semimembranosus muscles were subjected to a hydrostatic pressure of 100 meganewtons/m(2) at 25°C. The ultrastructure of the muscle fibres was compared with that of non pressure-treated samples. A conspicuous feature of pressure-treated post-rigor samples was the absence of the M-band in the central region of the A-band. Therefore it appeared that some, if not all, of the proteins in the M-line were very susceptible to disaggregation under high pressure. Another feature of the post-rigor pressure-treated sample was the loss of integrity and aggregation of I-band filaments which presumably involved an F-G transformation of actin. Pressure treatment of pre-rigor muscle resulted in extensive structural disruption with contraction band formation. It is suggested that a weakening of thin filaments and M-line bridges, when combined with a pressure-induced contraction, facilitates disruption of pre-rigor pressure-treated muscle.