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  • Title: Studies of a key protein in the mechanism of the excitation-contraction coupling process of frog skeletal muscle, using phenylglyoxal.
    Author: Fujino S, Satoh K, Nakai T, Togashi K, Kado T, Fujino M, Arima T, Fujino M.
    Journal: Experientia; 1993 Feb 15; 49(2):138-44. PubMed ID: 8440350.
    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, using 14C-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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