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The actin content of the myometrium

  • Biochemistry and Biophysics
  • Published:
Bulletin of Experimental Biology and Medicine Aims and scope

Summary

Proteins extracted by Weber's solution from the smooth muscle of the uterus do not possess the ability to interact with myosin preparations with the formation of actomyosin. This makes highly improbable the assumption of Snellman and Tenow on the presence of any appreciable amounts of free actin in 0.5 M KCL extracts of myometrium.

Investigations conducted by the method of paper electrophoresis demonstrate the presence of 3 fractions in the myometrium extracts with high ionic potential, viz., myoalbumin, heterogeneous myogen and actomyosin. The latter consists of a small quantity of actomyosin (undoubtedly bound with nucleoproteins) and water-soluble myofibrillar proteins (mainly tropomyosin and possibly Δ-protein). Likewise these investigations give no grounds for associating the peculiarity of the myometrial proteins with the high concentration of the “easily extractable” actin in the muscles of the uterus.

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Authors and Affiliations

  1. Biochemical Laboratory of the Institute of Obstetrics and Gynecology, AMN SSSR, Leningrad

    I. I. Ivanov & N. I. Mirovich

Authors
  1. I. I. Ivanov
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  2. N. I. Mirovich
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Ivanov, I.I., Mirovich, N.I. The actin content of the myometrium. Bull Exp Biol Med 48, 1110–1113 (1959). https://doi.org/10.1007/BF00868911

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  • DOI: https://doi.org/10.1007/BF00868911

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