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Physarum Tropomyosin-Troponin Complex

descriptionPublicationkeyboard_double_arrow_right Article 01 Sep 1975 English Publisher:Oxford University Press (OUP)Journal:The Journal of Biochemistry, volume 78, pages 583-588 (issn: 0021-924X, eissn: 1756-2651,

Authors: Yuji Tonomura; Toyoki Kato;

doi: 10.1093/oxfordjournals.jbchem.a130943

pmid: 131791

Physarum Tropomyosin-Troponin Complex

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Abstract

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.

Keywords

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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	impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.	Top 10%