A low calcium requiring form of calcium activated protease (LCAP)and a high calcium requiring form of calcium activated protease (HCAP), purified from porcine skeletal muscle, were studied. LCAPwas most active at pH 8.2. The HCAPwas rather unstable at high temperature or at alkaline pHs: The antiserum to purified LCAPdid not make a precipitin line with HCAP.Those proteases hydrolyzed myofibril proteins to disassemble the structure of myofibrils. The electronmicrogram of the myofibril treated by LCAPresembled that of the muscle obtained from a vitamin E deficient rat. Both LCAP and HCAPhydrolyzed purified a-actinin, liver actin, and some other proteins which are not assigned. The microsomeproteins were resistant to protease treatment, and only the 180kd protein was hydrolyzed by LCAP.
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