Professor Ebashi’s Journey Toward the Discovery of Troponin: A Personal Recollection

  • Makoto Endo
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 592)


I first met Dr. Setsuro Ebashi in 1954, when he was an instructor (or assistant professor) in the Department of Pharmacology, the University of Tokyo, and I was an undergraduate student. Our group of students was doing some experiments on dogs in the corner of the department, which Professor Ebashi had kindly allowed us to use. He was quite kindhearted, but when talking with him one immediately recognized his brilliance, and his penetrating eyes aroused a feeling of awe in us. I did not realize it then, but this was the time when he was establishing the fact that the essential principle of Marsh’s relaxing factor is not a soluble enzyme such as creatine kinase or myokinase, but a microsomal ATPase described by Kielley and Myerhof in 1948.1


Creatine Kinase Sarcoplasmic Reticulum Essential Principle Actomyosin ATPase Striation Pattern 
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2.1. References

  1. 1.
    H. Kumagai, S. Ebashi, and F. Takeda, Essential relaxing factor in muscle other than myokinase and creatine phosphokinase. Nature 176, 166–168 (1955).PubMedCrossRefGoogle Scholar
  2. 2.
    E. Bozler, Relaxation in extracted muscle fibers. J. Gen. Physiol. 38, 149–159 (1954).PubMedCrossRefGoogle Scholar
  3. 3.
    F. Ebashi, and S. Ebashi, On the substances that cause relaxation of glycerinated muscle. (in Japanese) Folia Pharmacol. Jap. 55, 31§ (1959).Google Scholar
  4. 4.
    S. Ebashi, Calcium binding and relaxation in the actomyosin system. J. Biochem. 48, 150–151 (1960).Google Scholar
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    S. Ebashi, Calcium binding activity of vesicular relaxing factor. J. Biochem. 50, 236–244 (1961).Google Scholar
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    S. Ebashi, and F. Lipmann, Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle. J. Cell Biol. 14, 389–400 (1962).CrossRefGoogle Scholar
  7. 7.
    S. Ebshi, The role of “relaxing factor” in contraction-relaxation cycle of muscle. Progr. Theoret. Phys. (Kyoto) Suppl. 17, 35–40 (1961)Google Scholar
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    A. Weber, On the role of calcium in the activity of adenosine 5′-triphosphate hydrolysis by actomyosin. J. Biol. Chem. 234, 2764–2769 (1959).PubMedGoogle Scholar
  9. 9.
    H. H. Weber, Introduction (to “Interaction of myosin and actin”), in: Biochemistry of Muscle Contraction, edited by J. Gergely (Little, Brown and Co., Boston, 1964), pp. 193–198.Google Scholar
  10. 10.
    A. Weber, and S. Winicur, The role of calcium in the superprecipitation of myosin. J. Biol. Chem. 236, 3198–3202 (1961).PubMedGoogle Scholar
  11. 11.
    S. Ebashi, Third component participating in the superprecipitation of “natural actomyosin.” Nature 200 1010 (1963).PubMedCrossRefGoogle Scholar
  12. 12.
    M. Endo, Comment. Proc. Roy. Soc. Lond. B160, 500 (1964).Google Scholar
  13. 13.
    S. Ebashi, and A. Kodama, A new protein factor promoting aggregation of tropomyosin. J. Biochem. 58, 107–108 (1965).PubMedGoogle Scholar
  14. 14.
    M. Endo, Y. Nonomura, T. Masaki, I. Ohtsuki, and S. Ebashi, Localization of native tropomyosin in relation to striation patterns. J. Biochem. 60, 605–608 (1966).Google Scholar

Copyright information

© Springer 2007

Authors and Affiliations

  • Makoto Endo
    • 1
  1. 1.Faculty of Medical Care and HealthSaitama Medical UniversityKawagoeJapan

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