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Studies of a key protein in the mechanism of the excitation-contraction coupling process of frog skeletal muscle, using phenylglyoxal

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Abstract

The excitation-contraction (E-C) coupling process in single twitch fibres from frog toe muscle was inhibited selectively by phenylglyoxal (PGO), a specific guanidyl modifying reagent. A new protein (31.5 kDa), which has PGO-binding ability and seems to play a key role in the E-C coupling process, was solubilized from transverse tubule membrane-junctional sarcoplasmic reticulum complexes (TTM-JSR) of frog skeletal muscles, using14C-PGO. The monoclonal antibody against this protein applied extracellularly inhibited the E-C coupling process of the single fibres. This protein appears to constitute the very first step of input for E-C coupling. It is considered to behave as an indispensable part of an ‘electrometer’ to measure membrane potentials. Therefore, the name ‘electrometrin’ is suggested for the new protein.

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Authors and Affiliations

  1. Department of Pharmacology, Hokkaido Institute of Pharmaceutical Sciences, Otaru, (Japan)

    S. Fujino, K. Satoh, T. Nakai, K. Togashi & T. Kado

  2. Department of Pharmacology, Sapporo Medical College, Sapporo, (Japan)

    M. Fujino

  3. Department of Physiology, National Defense Medical College, Tokorozawa, Saitama, (Japan)

    T. Arima & M. Fujino

Authors
  1. S. Fujino
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  2. K. Satoh
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  3. T. Nakai
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  4. K. Togashi
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  5. T. Kado
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  6. M. Fujino
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  7. T. Arima
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  8. M. Fujino
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Fujino, S., Satoh, K., Nakai, T. et al. Studies of a key protein in the mechanism of the excitation-contraction coupling process of frog skeletal muscle, using phenylglyoxal. Experientia 49, 138–144 (1993). https://doi.org/10.1007/BF01989418

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  • DOI: https://doi.org/10.1007/BF01989418

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