Biochemical Studies on Contractile and Regulatory System of Muscle from Cestode.

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Structural, contractile and regulatory proteins were isolated from whole body of a cestode, Spirometra erinacei. The present report describes the preparation and some characteristics of the isolated proteins. 1. Myofibril-like materials were prepared from ablut and larval (plerocercoid) worms. Myosin, actin and paramyosin (PM) were detected in the materials by the method of SDS-gel electrophoresis. 2. PM, structural protein, was purified from acetone-treated powder of anolt and larval worms. Both the purified proteins formed paracrystal structures with regular axial banding patterns on electron micrographs. 3. Natural actomyosin (myosin B) were extracted from adult and larval myofibril treated by 0.05 M NaCl containing various protease inhibitors and non-ionic detergent. Both the myosin B isolated had high ATPase activity. 4. The adult myosin B was found be Ca^<2+>-sensitive based on superprecipitation. 5. Troponin(TN)-tropomyosin(TM) complex(nTM) was isolated by the extraction with 0.4 M LiCl and acidification for denatulation of actomyosin. The isolated nTM conferred high Ca^<2+>-sensitivity on the superprecipitation and Mg^<2+>-ATPase activity of reconstituted vertebrate skeletal actomysin. This result suggested at least that the cestode had a regulatory protein located on actin filaments. The purification on TN and TM is currently in progress.