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Solubilization, Physiological Role, and Localization of a Key Protein (31.5 KD) to Excitation-Contraction Coupling Process of Frog Skeletal Muscle Cells, Using Phenylglyoxal

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Excitation-Contraction Coupling in Skeletal, Cardiac, and Smooth Muscle

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 311))

Summary

A new phenylglyoxal-binding protein (31.5 kD) was solubilized from frog skeletal muscle. The monoclonal AB against the 31.5 kD protein inhibited extracellularly E-C coupling process of single-muscle fibers.

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References

  1. Fujino, M. et al.; J. Physiol., Soc. Japan., 45: 507 (1983).

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  2. Fujino, M. et al.; Proc. Int. Union Physiol., 16:207, (1986).

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  3. Takahashi, K.; J. Biol. Chem., 243:6171 (1968).

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  4. Fujino, S. et al.; Experientia, 45:467, (1989).

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© 1992 Springer Science+Business Media New York

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Fujino, S. et al. (1992). Solubilization, Physiological Role, and Localization of a Key Protein (31.5 KD) to Excitation-Contraction Coupling Process of Frog Skeletal Muscle Cells, Using Phenylglyoxal. In: Frank, G.B., Bianchi, C.P., ter Keurs, H.E.D.J. (eds) Excitation-Contraction Coupling in Skeletal, Cardiac, and Smooth Muscle. Advances in Experimental Medicine and Biology, vol 311. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3362-7_31

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  • DOI: https://doi.org/10.1007/978-1-4615-3362-7_31

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6483-2

  • Online ISBN: 978-1-4615-3362-7

  • eBook Packages: Springer Book Archive

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