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The action of a high pressure on the adenosinetriphatase activity of myosin

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

Summary

Solutions of reprecipitated myosin lose completely their adenosinetriphosphates activity under the effect of high pressure (4000 atmospheres). However, they retain their ability to readily dissolve in 0.6 M KCl and to become precipitated in subsequent dialysis or after considerable dilution of myosin salt solution with water. The viscosity of myosin, free of actomyosin admixture, rises under the effect of high pressure. Myosin subjected to the effect of high pressure loses its ability to combine with an activated actin with the formation of actomyosin. The viscosity of actomyosin gels subject to high pressure (4000 atmospheres) does not diminish after addition of adenosinetriphosphates. Under the effect of high pressure there must occur some kinds of changes in the myosin structure, these being associated with inactivation of certain groups (possibly SH) and imparting to myosin an enzymatic character without, however, making it lose its hydrophilic properties.

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Authors and Affiliations

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

    I. I. Ivanov, N. I. Mirovich & É. A. Parshina

  2. Department of Biochemistry of the Leningrad Institute of Pediatric Medicine, Leningrad, USSR

    I. I. Ivanov, N. I. Mirovich & É. A. Parshina

Authors
  1. I. I. Ivanov
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  2. N. I. Mirovich
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  3. É. A. Parshina
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Ivanov, I.I., Mirovich, N.I. & Parshina, É.A. The action of a high pressure on the adenosinetriphatase activity of myosin. Bull Exp Biol Med 47, 690–692 (1959). https://doi.org/10.1007/BF00781221

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  • DOI: https://doi.org/10.1007/BF00781221

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