Studies of a key protein in the mechanism of the excitation-contraction coupling process of frog skeletal muscle,using phenylglyoxal |
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| Authors: | S. Fujino K. Satoh T. Nakai K. Togashi T. Kado M. Fujino T. Arima M. Fujino |
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| Affiliation: | (1) Department of Pharmacology, Hokkaido Institute of Pharmaceutical Sciences, Otaru, (Japan);(2) Department of Pharmacology, Sapporo Medical College, Sapporo, (Japan);(3) Department of Physiology, National Defense Medical College, Tokorozawa, Saitama, (Japan) |
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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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| Keywords: | Frog skeletal single fibres phenylglyoxal (PGO) E-C coupling solubilization PGO-binding protein (PGO-protein) monoclonal antibody electrometrin |
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