Muscle Physiology and Biochemistry by Shoichi Imai, Makoto Endo, Iwao Ohtsuki

By Shoichi Imai, Makoto Endo, Iwao Ohtsuki

The papers during this quantity have been contributed via shut buddies, co-workers and scholars of Professor Setsuro Ebashi. they're devoted to him to commemorate his nice and pioneering contribution to the development of muscle body structure and biochemistry, which, in time, exerted a superb impact customarily box of lifestyles technological know-how. We think that this factor finds the current kingdom of analysis on muscle and/or calcium that used to be spread out by way of Professor Ebashi.

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Biophys J 72: A60, 1997 79. Zang R, Sheng Z, Jones M, Parsons B, Potter JD: Effect of mutations in the inhibitory region of skeletal muscle troponin I on its biological activity. Biophys J 70: A 165, 1996 80. Van Eyk JE, Thomas LT, Tripet, B, Wiesner RJ, Pearlstone JR, Farah CS, Reinach FC, Hodges RS: Distinct regions of troponin I regulate Ca'·-dependent activation and Ca'· sensitivity of the acto-SI-TMATPase activity ofthin filaments. J Bioi Chern 272: 10529-10537,1997 81. Tripet B, Van Eyk JE, Hodges RS: Mapping of a second actintropomyosin and a second troponin C binding site within the C terminus oftroponin I and their importance in the Ca'·-dependent regulation of muscle contraction.

Biochem Biophys Acta 368: 247-258, 1974 33. Regenstein JM, Szent-Gyorgyi AG: Regulatory proteins of lobster striated muscle. Biochemistry 14: 917-925,1975 34. Lehman W, Regenstein JM, Ransom AL: The stoichiometry of the components of arthropod thin filaments. Biochem Biophys Acta 434: 215-222,1976 35. Kobayashi T, Takagi T, Konishi K, Cox JA: Amino acid sequence of crayfish troponin I. J BioI Chern 264: 1551-1557, 1989 36. Shinoda Y, Yamada A, Yagi, K: Identification oftroponin I of crayfish myofibrils.

36 the exchange of the endogenous troponin T 2f with another isofonn (troponin T 1f), and vice versa, in the myofibrils [33] and also after the exchange ofthe whole endogenous troponin T with its fragments devoid of the N-tenninal residues in the myofibrils [32] and the skinned fibers [34]. The N-tenninal region oftroponin T is therefore by no means involved in the Ca2+-activation profiles ofcontraction including cooperativity. The troponin T , subfragment itself shows the strong inhibitory action on actomyosin ATPase activity in the presence of tropomyosin-troponin I·C regardless of Ca 2+concentrations [25].

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