Pressure-Induced Changes in Myofibrillar Proteins

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Abstract
Natural actomyosin, synthetic actomyosin, myosin and F-actin were subjected to lactoperoxidase-catalyzed iodination with 125I before and after exposure to a pressure of 150 mNm-2. After iodination, myosin was split into its subfragments, light and heavy meromyosin, and the actomyosins were separated into their component proteins. The effect of the pressure treatment on the extent of I incorporation into both the light and heavy chains of myosin and into actin depended on whether the myosin and actin were present as components of natural or synthetic actomyosin or in the purified state. Conformational changes altering the exposure of tyrosine groups are induced in isolated myosin and actin by pressure treatment and are partly prevented when these proteins are combined in synthetic actomyosin and more completely prevented when they are combined in natural actomyosin.