By Karl Marx, Musto
Socialism and Democracy, 2014
Vol. 28, No.2, 39-58
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Extra resources for Documents from the International Workingmen's Association
Weber and her colleagues (see 1), as well as the possible interaction among myosin molecules involving the domains of different tropomyosin molecules has to be further explored. Actin, which usually has been regarded as playing a passive role in the interaction with myosin, may have dynamic properties, as revealed by recent studies utilizing quasi-elastic light scattering (22) and electron spin resonance (23, 24), that deserve greater consideration in our thinking about contraction and regulatory mechanisms.
Ed. L. M. G. , J. C. Ruegg and Th. Wietand, pp. 9-25 (Berlin 1976). 22. , S. Quasi Elastic Light Scattering of Laser Light. J. Molec. BioI. 62, 251 (1971). 23. , G. H. Reed, and A. Weber: Conformational Change and Cooperativity in Actin Filaments Free of Tropomyosin. Proc. Nat. Acad. Sci. ) 72, 3412 (1975). 24. Thomas, D. , J. C. Seidet, J. Gergety: Rotational Dynamics of F-actin Studied by Saturation Transfer EPR Spectroscopy. Fed. Proc. 35, 1746 (1976). 25. Engtand, P. : Correlation between Contraction and Phosphorylation of the Inhibitory Subunit of Troponin in Perfused Rat Heart.
Zusatzlich wird der hemmende Effekt von anorganischem Phosphat auf die kontraktile Spannung im Zusammenhang mit der Entstehung der energetischen Insuffizienz diskutiert. References 1. , H. J. Doring, J. Janker, Y. K. Byon: Basic actions of ions and drugs on myocardial high-energy phosphate metabolism and contractility. In: Handbook of experimental pharmocology, New Series, Vol. : J. Schmier, O. Eichler (Berlin-Heidelberg-New York 1975). 2. Gillis, J. , G. Mankhal: The incorporation of radioactive phosphate into ATP in glycerinated fibres stretched or released during contraction.