Physarum tropomyosin-troponin complex. Isolation and properties.
Copyright policy )Physarum tropomyosin-troponin complex. Isolation and properties.
The relaxing protein (TM-TN complex) was isolated from plasmodia of Physarum. SDS-gel electrophoresis revealed that the relaxing protein consists of tropomyosin subunits with a molecular weight of 35,000 troponin subunits with molecular weights of 38,000 (T) and 24,000 (I) and several other components. No component corresponding to muscle troponinC (MW-18,000) was detected in the plasmodium relaxing protein. The relaxing protein combined with muscle F-actin, and inhibited the ATPase [EC 3.6.1.3] activity and superprecipitation of reconstituted muscle actomysin in the absence of Ca2+ ions. The inhibition was reversed by adding 1 muM Ca2+ ions.
Adenosine Triphosphatases, Binding Sites, Macromolecular Substances, Muscles, Muscle Proteins, Tropomyosin, Actins, Troponin, Enzyme Activation, Molecular Weight, Physarum, Animals, Calcium, Myxomycetes, Rabbits, Muscle Contraction, Protein Binding
Adenosine Triphosphatases, Binding Sites, Macromolecular Substances, Muscles, Muscle Proteins, Tropomyosin, Actins, Troponin, Enzyme Activation, Molecular Weight, Physarum, Animals, Calcium, Myxomycetes, Rabbits, Muscle Contraction, Protein Binding
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