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Contractility and ATPase activity of myofibrlls from normal and PSE porcine muscles were studied Studies were also made on the extractability of proteins from myofibrils isolated from normal and PSE muscles. Normal muscles contracted instantaneously after the addition of Mg '+-ATP, while PSE muscles contracted in part or did not contract. ATF'ase activity of myofibrils isolated from muscle having higher pH value was higher than that of myofibrils isolated from muscle having lower pH value. When using either Hasselbach-Schneider or KI solutions to extract myoflbrillar proteins, the proportion of protein extracted was significantly higher for normal muscles when compared to those from PSE muscles.

Several workers have documented that rabbit "ghost" fibers and myofibrils irrigated with myosin can contract upon addition of Mg2+-ATP.1•`5) Tawada et al.5) have indicated that in the myosin-irrigated fibers thick filaments are reformed in lengths from one Z-mem brane to the other Z-membrane of a sarcomere, running

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