Pressures of the order of 100 MNm'* applied for 2.5 min or longer to postrigor muscle heated to 40-60"~ improved the tenderness of the meat when subsequently cooked. The magnitude of the effect depended on the intensity and duration of pressurization, and the temperature attained by the meat during pressurization. As judged by taste panel assessment and by shear values of the cooked meat, the properties of pressure-heat treated postrigor muscle approximated those of prerigor pressurized muscle. The process is effective in overcoming toughness associated with contracted muscle. It is suggested that the treatment operates on the myofibrillar component of toughness.

A method has been developed for preparation of purified desmin from mature mammalian (porcine) skeletal muscle. A crude desmin-containing fraction was prepared by modification of procedures used for isolation of smooth-muscle intermediate-filament protein [Small & Sobieszek (1977) J. Cell Sci. 23, 243-268]. The desmin was extracted in 1 M-acetic acid/20 mM-NaCl at 4 degrees C for 15h from the residue remaining after actomyosin extraction from washed myofibrils. Successive chromatography on hydroxyapatite and DEAE-Sepharose CL-6B in 6M-urea yielded desmin that was routinely more than 97% 55 000-dalton protein and that had no detectable actin contamination. Removal of urea by dialysis against 10mM-Tris/acetate (pH 8.5)/1 mM dithioerythritol and subsequent clarification at 134 000 g (rav. 5.9 cm) for 1 h results in a clear desmin solution. Dialysis of purified desmin against 100 mM-NaCl/1 mM-MgCl2/10 mM-imidazole/HCl, pH 7.0, at 2 degrees C resulted in the formation of synthetic desmin filaments have an average diameter of 9-11.5 nm. The present studies demonstrate that the relatively small amount of desmin in mature skeletal muscle can be isolated in sufficient quantity and purity to permit detailed studies of its properties and function. Although 10nm filaments have not been unequivocally demonstrated in mature muscle in vivo, that the purified skeletal-muscle desmin will form 10 nm filaments in vitro lends support to their possible existence and cytoskeletal function in mature skeletal-muscle cells.

No abstract

Risk factors for rhabdomyolysis featured in nearly all of the reports of statin-associated rhabdomyolysis and the majority of reports listed multiple risk factors, although dependence on risk factors appeared to be stronger with simvastatin than atorvastatin. The multiplication of risk factors in patients taking simvastatin and atorvastatin should be minimised.

Instron compression, Warner-Bratzler peak shear force and adhesion measurements, together with subjective assessments, have been used to determine the effectiveness of a pressure-heat treatment in improving the tenderness of post-rigor muscles widely varying in connective tissue content. Both shear force and compression values were decreased by the treatment, the effect being greater on peak shear force values. It had little or no effect on adhesion values, which reflect connective tissue strength. The juiciness of the pressure-heat treated samples was significantly less than that of the controls. It was shown that although peak shear force values were considerably reduced, the tenderness of the treated samples was limited by connective tissue toughness.