Biochemical Studies on Contractile and Regulatory System of Muscle from Cestode.
| Project/Area Number |
01570220
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
寄生虫学(含医用動物学）
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| Research Institution | KIATASATO UNIVERSITY |
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Principal Investigator |
NAKAMURA Takeshi Kitasato University, School of Medicine, Assistant professor., 医学部, 講師 (30050652)
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| Co-Investigator(Kenkyū-buntansha) |
KAWAKAMI Yasushi Azabu University, School of Enviroionmental Biology, Assistant professor., 環境保健学部, 助手 (80204684)
YNAHISAWA Toshio Kitasato University, School of Medicine, Professor., 医学部, 教授 (20050312)
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| Project Period (FY) |
1989 – 1990
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| Project Status |
Completed (Fiscal Year 1990)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1990: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1989: ¥1,300,000 (Direct Cost: ¥1,300,000)
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| Keywords | Cestode / Spirometra erinacei / Muscle contraction / Actomyosin / Calcium regulation / Troponin / Cestoda / Paramyosin / Ca^<2+>-regulation |
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| Research Abstract |
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.
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Report
(3 results)
Research Products
(3 results)
